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Proteins in PDB homologous to 2vssA

Additional 2vss chains
2vssB

105 proteins (543 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 70
%M
75
&Y
120
%G
2j5iB, 2j5iC, 2j5iD, 2j5iE, 2j5iF, 2j5iG, 2j5iH, 2j5iJ, 2j5iK, 2j5iL, 2vssA, 2vssB, 2vssC, 2vssDHydroxycinnamoyl-Coa Hydratase-Lyase4.1.2.41, 4.2.1.1011.1e-11797.2247 %M&Y%G
2vssFWild-Type Hydroxycinnamoyl-Coa Hydratase1.8e-11796.8247 %M&Y%G
2vsuCA Ternary Complex Of Hydroxycinnamoyl-Co2.2e-11796.8247 %M&Y%G
2vsuA, 2vsuB, 2vsuDA Ternary Complex Of Hydroxycinnamoyl-Co2.2e-11796.8247 %M&Y%G
2j5iIHydroxycinnamoyl-Coa Hydratase-Lyase2.2e-11796.8247 %M&Y%G
2vsuFA Ternary Complex Of Hydroxycinnamoyl-Co3.8e-11796.4247 %M&Y%G
2j5iAHydroxycinnamoyl-Coa Hydratase-Lyase4.5e-11796.8247 %M&Y%G
2vssEWild-Type Hydroxycinnamoyl-Coa Hydratase1.1e-11696.8247 %M&Y%G
2vsuEA Ternary Complex Of Hydroxycinnamoyl-Co2.3e-11696.4247 %M&Y%G
2iexA, 2iexB, 2iexCDihydroxynapthoic Acid Synthetase (Gk2871.7e-2636.9217 %G&R%G
2uzfA, 2uzfBStaphylococcus Aureus 1,4-Dihydroxy-2- N4.1.3.369e-2435.1211 %G--%G
2pbpA, 2qq3A, 2qq3B, 2qq3C, 2qq3D, 2qq3E, 2qq3F, 2qq3G, 2qq3H, 2qq3I, 2qq3J, 2qq3K, 2qq3LEnoyl-Coa Hydrates Subunit I (Gk_2039) F5.3e-2229.5244 %A&M%G
1uiyAEnoyl-Coa Hydratase From Thermus Thermop7.4e-2234.3210 %A&L%G
4elsA, 4elsB, 4elsC, 4elsD, 4elsE, 4elsF, 4elwA, 4elwB, 4elwC, 4elwD, 4elwE, 4elwF, 4elxA, 4elxB, 4elxC, 4elxD, 4elxE, 4elxF, 4i42A, 4i42B, 4i42C, 4i42D, 4i42E, 4i42F, 4i42G, 4i42H, 4i42I, 4i42J, 4i42K, 4i42LE. Coli. 1,4-Dihydroxy-2- Naphthoyl Coen4.1.3.368.6e-2234.6205 %G&R%G
3t88A, 3t88B, 3t88C, 3t88D, 3t88E, 3t88F, 3t89A, 3t89B, 3t89C, 3t89D, 3t89E, 3t89FEscherichia Coli Menb In Complex With Su4.1.3.368.7e-2234.6205 %G&R%G
1jxzA, 1jxzB, 1jxzCThe H90q Mutant Of 4-Chlorobenzoyl-Coenz3.8.1.71.4e-2031.8220 %F&I%G
1ey3A, 1ey3B, 1ey3C, 1ey3D, 1ey3E, 1ey3FEnoyl-Coa Hydratase Complexed With The S4.2.1.171.6e-2031.0213 %A&M%G
1mj3A, 1mj3B, 1mj3C, 1mj3D, 1mj3E, 1mj3FCrystal Structure Analysis Of Rat Enoyl-4.2.1.171.6e-2031.0213 %A&M%G
1dubA, 1dubB, 1dubC, 1dubD, 1dubE, 1dubF, 2dubA, 2dubB, 2dubC, 2dubD, 2dubE, 2dubF2-Enoyl-Coa Hydratase, Data Collected At4.2.1.171.6e-2031.0213 %A&M%G
4emlA, 4emlB, 4emlC, 4emlD, 4emlE, 4emlF, 4i4zA, 4i4zB, 4i4zC, 4i4zD, 4i4zE, 4i4zF, 4i4zG, 4i4zH, 4i4zI, 4i52A, 4i52B, 4i52C, 4i52D, 4i52E, 4i52F, 4i52G, 4i52H, 4i52ISynechocystis Sp. Pcc 6803 1,4-Dihydroxy2.5e-2033.0212 %G--%G
3moyAProbable Enoyl-Coa Hydratase From Mycob 3.4e-2030.4230 %A&M%G
1nzyA, 1nzyC4-Chlorobenzoyl Coenzyme A Dehalogenase 3.8.1.74.2e-2031.4220 %F&I%G
1nzyB4-Chlorobenzoyl Coenzyme A Dehalogenase 3.8.1.75e-2031.4220 %F&I%G
2hw5A, 2hw5B, 2hw5C, 2hw5D, 2hw5E, 2hw5FThe Human Enoyl-Coenzyme A (Coa) Hydrata4.2.1.176.5e-2030.2212 %A&M%G
3kqfA, 3kqfB, 3kqfC, 3kqfD, 3kqfE, 3kqfF1.8 Angstrom Resolution Enoyl-Coa Hydrat5.1e-1932.7202 %A&R%G
3pzkA, 3pzkB, 3pzkC, 3q0gA, 3q0gB, 3q0gC, 3q0gD, 3q0gE, 3q0gFThe Mycobacterium Tuberculosis Crotonase4.2.1.175.9e-1929.1234 %A&M%G
3q0jA, 3q0jB, 3q0jC, 3q0jD, 3q0jE, 3q0jFThe Mycobacterium Tuberculosis Crotonase5.9e-1929.1234 %A&M%G
3h81A, 3h81B, 3h81CEnoyl-Coa Hydratase From Mycobacterium T4.2.1.176.5e-1929.1234 %A&M%G
3h02A, 3h02B, 3h02C, 3h02D, 3h02E, 3h02F2.15 Angstrom Resolution Naphthoate Synt4.1.3.361.7e-1832.7205 %G&R%G
1dciA, 1dciB, 1dciCDienoyl-Coa Isomerase1.9e-1825.4240 %I&M%G
2vreA, 2vreB, 2vreCHuman Peroxisomal Delta3,5, Delta2,4-Die1e-1727.7238 %I&M%G
3rsiA, 3rsiB, 3rsiCThe A Putative Enoyl-Coa HydrataseISOMER1.6e-1728.0236 %G&W%G
2ej5A, 2ej5BGk2038 Protein (Enoyl-Coa Hydratase Subu1.8e-1728.5228 %E&V%A
3r0oA, 3r0oB, 3r0oCCarnitinyl-Coa Hydratase From Mycobacter1.9e-1729.9211 %A&I%G
3qkaA, 3qkaB, 3qkaC, 3qkaD, 3qkaE, 3qkaFEnoyl-Coa Hydratase Echa5 From Mycobacte3.1e-1728.6210 %A&F%G
3i47APutative Enoyl Coa HydrataseISOMERASE (C2.8e-1629.7209 %A&M%G
3qxiA, 3qxiB, 3qxiCEnoyl-Coa Hydratase Echa1 From Mycobacte8.1e-1628.0218 %M&F%G
3swxA, 3swxB, 3swxCA Probable Enoyl-Coa HydrataseISOMERASE 8.1e-1629.7212 %L&V%L
3qxzA, 3qxzB, 3qxzCA Probable Enoyl-Coa HydrataseISOMERASE 9.8e-1628.4197 %A&A%I
3trrA, 3trrB, 3trrC, 3trrD, 3trrE, 3trrFA Probable Enoyl-Coa HydrataseISOMERASE 1.1e-1526.2210 %M&F%G
3r9tA, 3r9tB, 3r9tCEcha1_1 From Mycobacterium Paratuberculo1.2e-1529.5210 %A&I%G
1q51A, 1q51B, 1q51C, 1q51D, 1q51E, 1q51F, 1q51G, 1q51H, 1q51I, 1q51J, 1q51K, 1q51L, 1q52A, 1q52B, 1q52C, 1q52D, 1q52E, 1q52F, 1q52G, 1q52H, 1q52I, 1q52J, 1q52K, 1q52LMycobacterium Tuberculosis Menb In Compl4.1.3.361.2e-1529.7229 %G&Y%G
3tlfA, 3tlfB, 3tlfC, 3tlfD, 3tlfE, 3tlfFAn Enoyl-Coa HydrataseISOMERASE FROM Myc1.2e-1527.9219 %A&I%A
3t8aA, 3t8aB, 3t8aC, 3t8bA, 3t8bBMycobacterium Tuberculosis Menb In Compl4.1.3.361.3e-1529.7229 %G&Y%G
1rjmA, 1rjmB, 1rjmC, 1rjnA, 1rjnB, 1rjnCMenb (rv0548c) From Mycobacterium Tuberc4.1.3.361.3e-1529.7229 %G&Y%G
3r9sA, 3r9sB, 3r9sCA Carnitinyl-Coa Dehydratase From Mycoba1.4e-1529.5210 %A&I%G
4di1A, 4di1B, 4di1CEnoyl-Coa Hydratase Echa17 From Mycobact2.1e-1528.4211 %D&L%A
4f47AThe Enoyl-Coa Hydratase Echa19 From Myco3e-1529.0207 %M--%G
3omeA, 3omeB, 3omeC, 3omeD, 3omeE, 3omeFA Probable Enoyl-Coa Hydratase From Myco3.1e-1530.6209 %H&E%G
3r9qA, 3r9qB, 3r9qCA Probable Enoyl-Coa HydrataseISOMERASE 1.2e-1429.7195 %A&M%G
3t3wA, 3t3wB, 3t3wC, 3t3wD, 3t3wE, 3t3wFProbable Enoyl-Coa Hydratase From Mycoba1.3e-1430.6216 %H--%G
2vx2A, 2vx2B, 2vx2C, 2vx2D, 2vx2E, 2vx2F, 2vx2G, 2vx2H, 2vx2IHuman Enoyl Coenzyme A Hydratase Domain-6.8e-1428.4204 %H&L%A
3hrxA, 3hrxB, 3hrxC, 3hrxD, 3hrxE, 3hrxFPhenylacetic Acid Degradation Protein Pa6.9e-1430.3195 %Q&F%A
3oc7AAn Enoyl-Coa Hydratase From Mycobacteriu1.1e-1328.0207 %A&A%G
3gkbA, 3gkbB, 3gkbCA Putative Enoyl-coa Hydratase From Stre1.4e-1329.2219 %V&G%G
3peaA, 3peaB, 3peaC, 3peaD, 3peaE, 3peaFEnoyl-Coa Hydratase From Bacillus Anthra2.1e-1325.7210 %A&F%G
3njbA, 3njbB, 3njdA, 3njdBEnoyl-Coa Hydratase From Mycobacterium S8.5e-1328.3226 %F&Y%G
3qreAAn Enoyl-Coa Hydratase Echa12_1 From Myc1.1e-1228.1196 %A--%I
3isaA, 3isaB, 3isaC, 3isaD, 3isaE, 3isaFPutative Enoyl-Coa HydrataseISOMERASE FR1.8e-1228.5200 %F&Y%A
1ef8A, 1ef8B, 1ef8C, 1ef9AMethylmalonyl Coa Decarboxylase4.1.1.412.2e-1223.7219 %H&L%G
2ppyA, 2ppyB, 2ppyC, 2ppyD, 2ppyE, 2ppyFEnoyl-Coa Hydrates (Gk_1992) From Geobac3.2e-1229.6206 %A&L%G
3lkeA, 3lkeB, 3lkeCEnoyl-Coa Hydratase From Bacillus Halodu3.8e-1223.3245 %P&L%G
3qyrA, 3qyrB, 3qyrC, 3qyrD, 3qyrE, 3qyrFEnoyl-Coa Hydratase Echa16_2 Mycobacteri4.3e-1228.1210 %L--%G
1hzdA, 1hzdB, 1hzdC, 1hzdD, 1hzdE, 1hzdF, 2zqqA, 2zqqB, 2zqqC, 2zqqD, 2zqqE, 2zqqF, 2zqrA, 2zqrB, 2zqrC, 2zqrD, 2zqrE, 2zqrFHuman Auh Protein, An Rna-Binding Homolo4.2.1.184.7e-1225.0224 %A&R%G
3mybA, 3mybB, 3mybCEnoyl-Coa Hydratase Mycobacterium Smegm5.1e-1228.0214 %H&M%A
3p85ACrystal Structure Enoyl-Coa Hydratase Fr5.6e-1228.1210 %L--%G
2f6qA, 2f6qB, 2f6qCThe Human Peroxisomal Delta3, Delta2 Eno5.3.3.87.1e-1228.7230 %N&F%I
3pe8AEnoyl-Coa Hydratase From Mycobacterium S9e-1226.1234 %L&L%G
3sllA, 3sllB, 3sllC, 3sllD, 3sllE, 3sllFA Probable Enoyl-Coa HydrataseISOMERASE 1.3e-1128.6185 %A&A%G
3hp0A, 3hp0B, 3hp0C, 3hp0D, 3hp0E, 3hp0FA Putative Polyketide Biosynthesis Enoyl1.4e-1125.9251 %A--%G
3qk8A, 3qk8B, 3qk8C, 3qk8D, 3qk8E, 3qk8FEnoyl-Coa Hydratase Echa15 From Mycobact1.4e-1123.6208 %G&I%A
2gtrA, 2gtrB, 2gtrCHuman Chromodomain Y-Like Protein2.3.1.484.7e-1125.8233 %L&F%L
3fduA, 3fduB, 3fduC, 3fduD, 3fduE, 3fduFA Putative Enoyl-Coa HydrataseISOMERASE 9.8e-1126.7187 %N&F%I
3qmjAEnoyl-Coa Hydratase Echa8_6 From Mycobac1.3e-1026.9219 %T&M%I
3he2A, 3he2B, 3he2CEnoyl-Coa Hydratase From Mycobacterium T4.2.1.171.4e-1023.6216 %A&D%A
2fbmA, 2fbmB, 2fbmCAcetyltransferase Domain Of Cdy12.3.1.481.6e-1024.1232 %L&F%L
3p5mA, 3p5mB, 3p5mC, 3p5mD, 3p5mE, 3p5mFAn Enoyl-Coa HydrataseISOMERASE FROM Myc1.6e-1025.6203 %G--%F
2fw2A, 2fw2B, 2fw2C, 2fw2D, 2fw2E, 2fw2FCatalytic Domain Of Cdy2.3.1.484.8e-1024.1232 %L&F%L
3g64A, 3g64B, 3g64CPutative Enoyl-Coa Hydratase From Strept6.3e-1026.8213 %G&I%A
2j5gA, 2j5gB, 2j5gC, 2j5gE, 2j5gF, 2j5gG, 2j5gH, 2j5gI, 2j5gJ, 2j5gK, 2j5gL, 2j5sA, 2j5sBThe Native A Beta-Diketone Hydrolase Fro7e-1025.1219 %I&L%H
3l3sA, 3l3sB, 3l3sC, 3l3sD, 3l3sE, 3l3sF, 3l3sG, 3l3sH, 3l3sI, 3l3sJ, 3l3sK, 3l3sLAn Enoyl-Coa HydrotaseISOMERASE FAMILY P7e-1028.1224 %H&I%A
2j5gDThe Native A Beta-Diketone Hydrolase Fro7e-1025.1219 %I&L%H
3q1tA, 3q1tB, 3q1tC, 3q1tD, 3q1tE, 3q1tFEnoyl-Coa Hydratase From Mycobacterium A7.5e-1023.7186 %F&E%A
1sg4A, 1sg4B, 1sg4CHuman Mitochondrial Delta3-delta2- Enoyl5.3.3.88.3e-1026.8190 %L&M%G
2wtbAArabidopsis Thaliana Multifuctional Prot1.1.1.35, 4.2.1.17, 5.1.2.3, 5.3.3.88.6e-1025.4213 %F&F%G
3rrvA, 3rrvB, 3rrvC, 3rrvD, 3rrvE, 3rrvFAn Enoyl-Coa HydrataseISOMERASE FROM Myc8.9e-1024.9237 %G&Y%L
1xx4ARat Mitochondrial 3,2-Enoyl-Coa5.3.3.81.4e-0930.0190 %L&M%G
2x58A, 2x58BThe Mfe1 Liganded With Coa1.1.1.35, 4.2.1.17, 5.3.3.81.5e-0925.7202 %A&F%G
3zw8A, 3zw8B, 3zw9A, 3zw9B, 3zwaA, 3zwaB, 3zwcA, 3zwcBRat Peroxisomal Multifunctional Enzyme T1.5e-0925.7202 %A&F%G
1szoA, 1szoB, 1szoC, 1szoD, 1szoE, 1szoF, 1szoG, 1szoH, 1szoI, 1szoJ, 1szoK, 1szoLCrystal Structure Analysis Of The 6-Oxo 1.7e-0924.2223 %I&F%A
1o8uA, 1o8uB, 1o8uC, 1o8uD, 1o8uE, 1o8uFThe 2 Angstrom 6-oxo Camphor Hydrolase: 2.4e-0924.2223 %I&F%H
3zwbA, 3zwbBRat Peroxisomal Multifunctional Enzyme T5.4e-0925.2202 %A&F%G
3h0uA, 3h0uB, 3h0uCA Putative Enoyl-Coa Hydratase From Stre5.7e-0925.5204 %A&P%A
3laoA, 3laoB, 3laoCEnoyl-Coa Hydratase From Pseudomonas Aer5.9e-0924.7231 %L&L%A
1wz8A, 1wz8B, 1wz8C, 1wz8D, 1wz8E, 1wz8FProbable Enoyl-Coa Dehydratase From Ther4.4e-0823.7198 %G&I%A
2q35AThe Y82f Variant Of Ech2 Decarboxylase D5.7e-0823.1199 ----%G
2a7kA, 2a7kB, 2a7kC, 2a7kD, 2a7kE, 2a7kF, 2a7kG, 2a7kH, 2a7kI, 2a81A, 2a81B, 2a81CCarboxymethylproline Synthase (carb) Fro1.5e-0728.4194 %G&V%M
2q2xA, 2q34AThe Ech2 Decarboxylase Domain Of Curf Fr4.1e-0723.1199 ----%G
1wdkA, 1wdkB, 1wdlA, 1wdlB, 1wdmA, 1wdmB, 2d3tA, 2d3tBFatty Acid Beta-Oxidation Multienzyme Co1.1.1.35, 4.2.1.17, 5.1.2.3, 5.3.3.84.6e-0724.3206 %A&F%G
3hinA, 3hinBPutative Enoyl-Coa Hydratase From Rhodop1.7e-0622.4205 %L&L%G
3bptAHuman Beta-Hydroxyisobutyryl-Coa Hydrola3.1.2.45.9e-0623.7224 %G&I%G
2pg8A, 2pg8B, 2pg8CR254k Mutanat Of Dpgc With Bound Substra6.1e-0524.0233 %I&L%G
2np9A, 2np9B, 2np9CA Dioxygenase In The Crotonase Superfami6.6e-0524.2236 %I&L%G
3r6hAAn Enoyl-Coa Hydratase (Echa3) From Myco7.2e-0524.9221 %F&L%M
3m6mA, 3m6mB, 3m6mC, 3m6nA, 3m6nB, 3m6nCRpff Complexed With Rec Domain Of Rpfc0.0001724.8149 %G&F%G

Proteins identified as mutant are highlighted in maroon. Conservative changes in active site residues, e.g. &K, are marked in green. Non-conservative changes to active site residues (&A) are highlighted in red. Library sequence residues identical to MACie active site residues are shown in grey.

Likewise, E.C. numbers identical to the MACiE protein are shown in grey; differences in black.


Homologs in PDB for MACiE ID:


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