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Proteins in PDB homologous to 1zk7A

Additional 1zk7 chains
1zk7B

100 proteins (384 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 9
&V
11
*G
14
*G
65
&E
136
*V
141
*R
1zk7A, 1zx9ATn501 Mera1.16.1.11.1e-183100.0467 &V*G*G&E*V*R
1ebdA, 1ebdBDihydrolipoamide Dehydrogenase Complexed1.8.1.47.4e-4735.0451 &V*G*P&H*T*N
2eq6A, 2eq6B, 2eq8A, 2eq8B, 2eq8D, 2eq8E, 2eq9A, 2eq9B, 2eq9D, 2eq9E, 2eq9G, 2eq9H, 2eq9J, 2eq9KLipoamide Dehydrogenase From Thermus The6.6e-4236.1462 &V*G*P&A*Y*S
1dxlA, 1dxlB, 1dxlC, 1dxlDDihydrolipoamide Dehydrogenase Of Glycin1.8.1.43.4e-4131.7464 &I*G*P&H*V*H
1lpfA, 1lpfBThree-Dimensional Lipoamide Dehydrogenas1.8.1.45.7e-4030.2463 &V*G*P&E*V*N
2r9zA, 2r9zB, 2rabA, 2rabBGlutathione Amide Reductase From Chromat1.8.1.162.8e-3934.0432 &A*G*S&D*L*H
2eq7A, 2eq7B, 2yquA, 2yquBLipoamide Dehydrogenase From Thermus The3.7e-3931.4449 &V*G*P&K*L*Y
2qaeA, 2qaeBCrystal Structure Analysis Of Trypanosom1.8.1.42.2e-3831.1472 &V*G*P&H*M*K
1gerA, 1gerB, 1getA, 1getBThe Glutathione Reductase From Escherich1.8.1.73.8e-3832.5449 --*G*S&M*I*H
3ladA, 3ladBRefined Lipoamide Dehydrogenase From Azo1.8.1.44.8e-3830.1462 &V*G*P&E*V*N
1zmcA, 1zmcB, 1zmcC, 1zmcD, 1zmcE, 1zmcF, 1zmcG, 1zmcH, 1zmdA, 1zmdB, 1zmdC, 1zmdD, 1zmdE, 1zmdF, 1zmdG, 1zmdH, 2f5zA, 2f5zB, 2f5zC, 2f5zD, 2f5zE, 2f5zF, 2f5zG, 2f5zH, 2f5zI, 2f5zJHuman Dihydrolipoamide Dehydrogenase Com1.8.1.45.5e-3829.5475 &V*G*P&G*V*N
1zy8A, 1zy8B, 1zy8C, 1zy8D, 1zy8E, 1zy8F, 1zy8G, 1zy8H, 1zy8I, 1zy8JThe Dihydrolipoamide Dehydrogenase And D1.8.1.47.4e-3829.5475 &V*G*P&G*V*N
3rnmA, 3rnmB, 3rnmC, 3rnmDThe The Subunit Binding Of Human Dihydro1.8.1.47.8e-3829.5475 &V*G*P&G*V*N
3ii4A, 3ii4BMycobacterial Lipoamide Dehydrogenase Bo1.8.1.41.5e-3731.0452 &V*G*P&K*S*N
1ojtADihydrolipoamide Dehydrogenase1.4e-3631.4474 &V*G*P&H*I*N
1bhyALow Temperature Middle Resolution P64k F1.7e-3631.4474 &V*G*P&H*I*N
1jehA, 1jehB, 1v59A, 1v59BYeast E3, Lipoamide Dehydrogenase1.8.1.41.9e-3629.7478 &I*G*P&G*T*H
1gesA, 1gesB, 1geuA, 1geuBAnatomy Of An Engineered Nad-Binding Sit1.8.1.72.4e-3631.6449 --*G*S&M*I*H
2a8xA, 2a8xBLipoamide Dehydrogenase From Mycobacteri1.8.1.45.2e-3630.5452 &V*G*P&K*S*N
1lvlAThe Refined Pseudomonas Putida Lipoamide1.8.1.41.4e-3530.2450 &I*G*P&T*I*H
3urhA, 3urhBA Dihydrolipoamide Dehydrogenase From Si2.6e-3430.3466 &V*G*P&H*V*N
3o0hA, 3o0hBGlutathione Reductase From Bartonella He8.3e-3430.6447 &V*G*S&K*I*K
1xanAHuman Glutathione Reductase In Complex W1.8.1.72.3e-3230.8438 &V*G*S&H*Y*H
3djgXCatalytic Cycle Of Human Glutathione Red1.8.1.72.4e-3230.8438 &V*G*S&H*Y*H
1bwcA, 2gh5A, 2gh5B, 1graA, 1grbA, 1greA, 1grfA, 3grsA, 4gr1A, 3djjA, 3dk4A, 3dk8A, 3dk9A, 1grhA, 3sqpA, 3sqpBHuman Glutathione Reductase Complexed Wi1.8.1.72.4e-3230.8438 &V*G*S&H*Y*H
2aaqACrystal Structure Analysis Of The Human 1.8.1.72.4e-3230.8438 &V*G*S&H*Y*H
2grtA, 3grtA, 4grtA, 5grtAHuman Glutathione Reductase A34e, R37w M1.8.1.74.9e-3230.6438 &V*G*S&H*Y*H
1grtAHuman Glutathione Reductase A34eR37W MUT1.8.1.75.1e-3230.6438 &V*G*S&H*Y*H
4dnaA, 4dnaBPutative Glutathione Reductase From Sino7.6e-3231.1425 &V*G*S&A*V*R
1k4qAHuman Glutathione Reductase Inactivated 1.8.1.77.6e-3230.5439 &V*G*S&H*Y*H
1gsnAHuman Glutathione Reductase Modified By 1.8.1.71.4e-3130.6438 &V*G*S&H*Y*H
1dncAHuman Glutathione Reductase Modified By 1.8.1.72.2e-3130.6438 &V*G*S&H*Y*H
1grgASubstrate Binding And Catalysis By Gluta1.8.1.72.2e-3130.6438 &V*G*S&H*Y*H
1xdiA, 1xdiBLpda (Rv3303c) From Mycobacterium Tuberc1.6.5.23.9e-3029.8477 &I*G*P&R*E*V
2wbaA, 2wbaBProperties Of Trypanothione Reductase Fr1.8.1.126.3e-2927.8472 &V*G*S&S*A*H
2woiA, 2woiB, 2woiC, 2woiD, 2wovA, 2wovB, 2wovC, 2wovD, 2wowA, 2wowB, 2wowC, 2wowD, 2wp5A, 2wp5B, 2wp5C, 2wp5D, 2wp6A, 2wp6B, 2wp6C, 2wp6D, 2wpcA, 2wpcB, 2wpcC, 2wpcD, 2wpeA, 2wpeB, 2wpeC, 2wpeD, 2wpfA, 2wpfB, 2wpfC, 2wpfDTrypanothione Reductase From Trypanosoma6.4e-2927.8472 &V*G*S&S*A*H
3dh9A, 3dh9BDrosophila Thioredoxin Reductase, Wild-T1.8.1.92.3e-2629.7464 &V*G*S&E*T*T
3dghA, 3dghBDrosophila Thioredoxin Reductase, C-Term1.8.1.92.3e-2629.7464 &V*G*S&E*T*T
2nvkXThioredoxin Reductase From Drosophila Me1.8.1.92.3e-2629.7464 &V*G*S&E*T*T
2hqmA, 2hqmBGlutathione Reductase Glr1 From The Yeas1.8.1.72.6e-2627.6438 &V*G*S&S*V*H
2x50A, 2x50BTrypanothione Reductase From Leishmania 3.5e-2526.3476 &V*G*S&E*D*Y
2jk6A, 2jk6B, 2w0hA, 2w0hB, 2yauA, 2yauB, 4adwA, 4adwB, 4apnA, 4apnBTrypanothione Reductase From Leishmania 3.5e-2526.3476 &V*G*S&E*D*Y
1typA, 1typBSubstrate Interactions Between Trypanoth1.8.1.123.8e-2526.5475 &V*G*S&E*A*Y
1tytA, 1tytBCrystal And Molecular Crithidia Fascicul1.8.1.123.8e-2526.5475 &V*G*S&E*A*Y
2tprA, 2tprBTrypanothione Reductase From Crithidia F1.8.1.121.1e-2426.8470 &V*G*S&E*A*Y
1feaA, 1feaB, 1feaC, 1feaD, 1febA, 1febB, 1fecA, 1fecBUnliganded Crithidia Fasciculata Trypano1.8.1.121.1e-2426.8470 &V*G*S&E*A*Y
3dgzAMouse Mitochondrial Thioredoxin Reductas1.8.1.91.2e-2429.2445 &V*G*S&D*T*H
1zdlA, 1zkqAMouse Thioredoxin Reductase Type 21.8.1.91.3e-2429.2445 &V*G*S&D*T*H
1h6vA, 1h6vB, 1h6vC, 1h6vD, 1h6vE, 1h6vFMammalian Thioredoxin Reductase1.8.1.91.7e-2428.2489 &I*G*S&D*V*R
4b1bA, 4b1bBPlasmodium Falciparum Oxidised Thioredox3e-2428.0461 &V*G*P&L*T*Y
2zz0A, 2zz0B, 2zz0C, 2zz0D, 2zzbA, 2zzbB, 2zzbC, 2zzbD, 2zzcA, 2zzcB, 2zzcC, 2zzcDHuman Thioredoxin Reductase I (Secys 4981.8.1.95.8e-2426.8489 &I*G*S&D*I*R
2j3nA, 2j3nB, 2j3nC, 2j3nD, 2j3nE, 2j3nFHuman Thioredoxin Reductase 11.8.1.95.9e-2426.8489 &I*G*S&D*I*R
3eanA, 3eanB, 3eanC, 3eanD, 3eanE, 3eanF, 3eaoA, 3eaoB, 3eaoC, 3eaoD, 3eaoE, 3eaoFRecombinant Rat Selenoprotein Thioredoxi1.8.1.98.7e-2427.9488 &I*G*S&D*V*R
3qfaA, 3qfaB, 3qfbA, 3qfbBThe Human Thioredoxin Reductase-Thioredo1.8.1.93e-2327.4456 &I*G*S&D*I*R
2cfyA, 2cfyB, 2cfyC, 2cfyD, 2cfyE, 2cfyFHuman Thioredoxin Reductase 11.8.1.93e-2327.4456 &I*G*S&D*I*R
2x8cA, 2x8cB, 2x8gA, 2x8hA, 2x99AThioredoxin Glutathione Reductase From S3.1e-2326.6489 &V*G*S&A*T*K
2v6oASchistosoma Mansoni Thioredoxin-Glutathi3.6e-2327.5448 &V*G*S&A*T*K
3h4kAThe Wild Type Thioredoxin Glutatione Red3.6e-2327.5448 &V*G*S&A*T*K
3l8kA, 3l8kBA Dihydrolipoyl Dehydrogenase From Sulfo4.6e-2325.3442 &V*G*G&L*E*Y
3ic9A, 3ic9B, 3ic9C, 3ic9DThe Dihydrolipoamide Dehydrogenase From 7.8e-2326.9465 &I*G*T&T--*R
1ndaA, 1ndaB, 1ndaC, 1ndaDThe Trypanosoma Cruzi Trypanothione Redu1.8.1.122.5e-2225.3471 &V*G*S&S*A*N
1onfAPlasmodium Falciparum Glutathione Reduct1.8.1.73.5e-2226.1490 &V*G*S&H*N--
1bzlA, 1bzlBTrypanosoma Cruzi Trypanothione Reductas1.8.1.121.5e-2125.0472 &V*G*S&S*A*H
1gxfA, 1gxfBTrypanosoma Cruzi Trypanothione Reductas1.8.1.121.5e-2125.0472 &V*G*S&S*A*H
1aogA, 1aogBTrypanosoma Cruzi Trypanothione Reductas1.8.1.121.7e-2125.1466 &V*G*S&S*A*H
3cgcA, 3cgcB, 3cgdA, 3cgdB, 3cgeA, 3cgeBPyridine Nucleotide Complexes With Bacil1.5e-1524.4476 &I*G*A----*R
1mo9A, 1mo9B, 1mokA, 1mokB, 1mokC, 1mokD, 2c3dA, 2c3dB, 2c3cA, 2c3cB, 3q6jA, 3q6jBNadph Dependent 2-Ketopropyl Coenzyme M 1.8.1.58.7e-1523.9476 &I*I*G&A*V*N
3kd9A, 3kd9B, 3kd9CPyridine Nucleotide Disulfide Oxidoreduc1.8.1.144.2e-1427.7343 --------*S*Y
3ntdA, 3ntdBThe Shewanella Loihica Pv-4 Nadh-Depende8.8e-1426.8482 &I*G*G--*Q*T
3cgbA, 3cgbBPyridine Nucleotide Complexes With Bacil1.4e-1224.9345 ----------*R
2bc0A, 2bc0BStructural Analysis Of Streptococcus Pyo1.4e-1224.9357 --------*V*K
2bc1A, 2bc1B, 2bcpA, 2bcpBStructural Analysis Of Streptococcus Pyo1.4e-1224.9357 --------*V*K
1nhsAAn L40c Mutation Converts The Cysteine-S1.11.1.19.7e-1228.1345 --------*V*K
1nhpACrystallographic Analyses Of Nadh Peroxi1.11.1.19.7e-1228.1345 --------*V*K
1nhqACrystallographic Analyses Of Nadh Peroxi1.11.1.19.7e-1228.1345 --------*V*K
1nhrAAn L40c Mutation Converts The Cysteine-S1.11.1.19.7e-1228.1345 --------*V*K
1joaA, 1npxA, 2npxANadh Peroxidase With Cysteine-Sulfenic A1.11.1.19.7e-1228.1345 --------*V*K
1joaA, 1npxA, 2npxANadh Peroxidase From Streptococcus Faeca1.11.1.19.7e-1228.1345 --------*V*K
1f8wANadh Peroxidase Mutant: R303m1.11.1.11.5e-1128.2347 --------*V*K
3ntaA, 3ntaBThe Shewanella Loihica Pv-4 Nadh-Depende2.1e-1126.1482 &I*G*G--*Q*T
3iwaAA Fad-Dependent Pyridine Nucleotide-Disu2.2e-1123.1415 ------&A*T*K
3nt6A, 3nt6BThe Shewanella Loihica Pv-4 Nadh-Depende2.5e-1126.1482 &I*G*G--*Q*T
2cduA, 2cduBThe Water-Forming Nad(P)h Oxidase From L2.8e-1123.6348 --------*T*K
3icrA, 3icrB, 3icsA, 3icsB, 3ictA, 3ictBOxidized Bacillus Anthracis Coadr-Rhd1.6e-0923.5464 &V*G*G--*Y*V
2v3aA, 2v3bARubredoxin Reductase From Pseudomonas Ae1.18.1.15.6e-0829.3328 --------*I*R
1xhcANadh Oxidase /nitrite Reductase From Pyr1e-0626.4265 ----------*T
1d7yA, 1f3pA, 2gqwA, 2gr0A, 2gr1A, 2gr2A, 2yvfA, 2yvgA, 2yvjA, 2yvjPNadh-Dependent Ferredoxin Reductase, Bph4.4e-0629.4235 --------*T*T
2gr3AFerredoxin Reductase, Bpha4 (Oxidized Fo4.4e-0629.4235 --------*T*T
3itjA, 3itjB, 3itjC, 3itjDSaccharomyces Cerevisiae Thioredoxin Red1.8.1.97.1e-0627.2327 ------&E*V*A
3d8xA, 3d8xBSaccharomyces Cerevisiae Nadph Dependent1.8.1.99e-0631.8223 --------*V*A
2q0kA, 2q0kB, 2q0lA, 2q0lB, 3ishA, 3ishB, 3ishCOxidized Thioredoxin Reductase From Heli1.8.1.92.4e-0526.2340 &I*G*P&N*T*S
1q1rA, 1q1rB, 1q1wA, 1q1wBPutidaredoxin Reductase From Pseudomonas5e-0527.5255 --------*A*R
3lb8A, 3lb8BThe Covalent Putidaredoxin Reductase- Pu5.1e-0527.5255 --------*A*R
3fg2PFerredoxin Reductase For The Cyp199a2 Sy7.1e-0523.8403 ------&Q*L*H
2q7vA, 2q7vBDeinococcus Radiodurans Thioredoxin Redu0.0001325.1346 &I*G*P&V*A*A
1vdcANadph Dependent Thioredoxin Reductase1.8.1.90.0002427.5211 --------*A*A
4gcmA, 4gcmBA Thioredoxine Reductase (Trxb) From Sta0.0002525.1339 &I*G*P--*L*A
3f8dA, 3f8dB, 3f8dC, 3f8dDSulfolobus Solfataricus Thioredoxin Redu0.0002725.0320 ------&E--*S
3f8pA, 3f8pB, 3f8pC, 3f8pD, 3f8rA, 3f8rB, 3f8rC, 3f8rDSulfolobus Solfataricus Trxr-B30.0003624.7320 ------&E--*S
3ctyA, 3ctyBT. Acidophilum Thioredoxin Reductase0.0004721.9342 &I*G*A&L*V--

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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