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Proteins in PDB homologous to 3dfrA

89 proteins (503 PDB structures) with E() < 0.001

Homologs in SwissProt


Acc   E.C. E() % id alen 21
&W
26
&D
116
&T
3dfrACrystal Structures Of Escherichia Coli A1.5.1.37e-79100.0162 &W&D&T
1ludA, 2hm9A, 2hqpA, 1ao8A, 1bzfA, 1disA, 1diuA, 2l28A, 2lf1ASolution Dihydrofolate Reductase Complex1.5.1.32.2e-7798.1162 &W&D&T
3jw5A, 3jw5B, 3jwcA, 3jwcB, 3jwfA, 3jwfB, 3jwkA, 3jwkBBacillus Anthracis (Y102f) Dihydrofolate1.6e-2339.3163 &W&E&T
3jw3A, 3jw3BBacillus Anthracis (F96i) Dihydrofolate 2.3e-2338.7163 &W&E&T
2qk8A, 3datAThe Anthrax Drug Target, Bacillus Anthra3.1e-2338.7163 &W&E&T
3s9uA, 3s9uB, 3sa1A, 3sa1B, 3sa2A, 3sa2B, 3saiA, 3saiBBacillus Anthracis Dihydrofolate Reducta3.2e-2338.7163 &W&E&T
3fl8A, 3fl8B, 3fl8C, 3fl8D, 3fl8E, 3fl8F, 3fl8G, 3fl8H, 3fl9A, 3fl9B, 3fl9C, 3fl9D, 3fl9E, 3fl9F, 3fl9G, 3fl9H, 4elbA, 4elbH, 4elbC, 4elbB, 4elbG, 4elbF, 4elbD, 4elbE, 4eleA, 4eleB, 4eleC, 4eleD, 4eleE, 4eleF, 4eleG, 4eleH, 4elfA, 4elfB, 4elfC, 4elfD, 4elfE, 4elfF, 4elfG, 4elfH, 4elgA, 4elgB, 4elgC, 4elgD, 4elgE, 4elgF, 4elgG, 4elgH, 4elhA, 4elhH, 4elhC, 4elhB, 4elhG, 4elhF, 4elhD, 4elhEB. Anthracis Dihydrofolate Reductase (Dh3.3e-2338.7163 &W&E&T
3e0bA, 3e0bBBacillus Anthracis Dihydrofolate Reducta3.3e-2338.7163 &W&E&T
3jvxA, 3jvxB, 3jwmA, 3jwmBBacillus Anthracis Dihydrofolate Reducta3.3e-2338.7163 &W&E&T
2kgkASolution Bacillus Anthracis Dihydrofolat3.4e-2338.7163 &W&E&T
1zdrA, 1zdrBDhfr From Bacillus Stearothermophilus6.9e-2239.6159 &W&D&T
3ix9A, 3ix9BStreptococcus Pneumoniae Dihydrofolate R1.5.1.31.8e-2037.7151 &W&E&T
3lg4A, 3lg4BStaphylococcus Aureus V31y, F92i Mutant 1.5.1.32.8e-1935.0157 &W&D&T
3m08AWild Type Dihydrofolate Reductase From S1.5.1.36.5e-1934.8164 &W&D&T
3f0bX, 3fq0A, 3fqcA, 3fqcB, 3fqzA, 3f0qX, 3f0sXStaphylococcus Aureus Dihydrofolate Redu9e-1935.0157 &W&D&T
3fyvX, 3fywX, 3frdX, 3freX, 3frfXStaph. Aureus Dhfr Complexed With Nadph 1.5.1.39.1e-1935.0157 &W&D&T
2w9gA, 2w9hAWild-Type Staphylococcus Aureus Dhfr In 1.5.1.39.2e-1935.0157 &W&D&T
3sr5XS. Aureus Dihydrofolate Reductase Comple1.5.1.39.7e-1935.0157 &W&D&T
3sqyX, 3srqX, 3srrX, 3srsX, 3sruX, 3srwXS. Aureus Dihydrofolate Reductase Comple1.5.1.39.8e-1935.0157 &W&D&T
3sgyA, 3sgyB, 3sh2A, 3sh2BStaphylococcus Aureus Dihydrofolate Redu9.8e-1935.0157 &W&D&T
3m09AF98y Tmp-Resistant Dihydrofolate Reducta1.5.1.31.3e-1834.1164 &W&D&T
3f0uX, 3fqfA, 3fqoA, 3fqvA, 3f0vX, 3f0xXStaphylococcus Aureus F98y Mutant Dihydr1.9e-1834.4157 &W&D&T
3fy8X, 3fy9X, 3fraX, 3frbXStaph. Aureus Dhfr Complexed With Nadph 1.5.1.31.9e-1834.4157 &W&D&T
3tq8A, 3tq9A, 3tqaA, 3tqbAThe Dihydrofolate Reductase (Fola) From 2.2e-1839.6139 &W&D&T
2w9sA, 2w9sB, 2w9sC, 2w9sD, 2w9sE, 2w9sF, 2w9tA, 2w9tBStaphylococcus Aureus S1:dhfr In Complex1.5.1.32.3e-1834.4151 &W&D&T
3i8aXStaphylococcus Aureus H30n, F98y Dihydro1.5.1.33.8e-1834.4157 &W&D&T
3ia4A, 3ia4B, 3ia4C, 3ia4D, 3ia5A, 3ia5BMoritella Profunda Dihydrofolate Reducta5.7e-1839.6154 &W&E&T
2zzaA, 2zzaBMoritella Profunda Dihydrofolate Reducta5.7e-1839.6154 &W&E&T
2w3vA, 2w3wAMycobacterium Avium Dihydrofolate Reduct6.2e-1743.7103 &W&D--
1df7A, 1dg5A, 1dg7A, 1dg8ADihydrofolate Reductase Of Mycobacterium1.5.1.31.1e-1541.7103 &W&D--
2cigADihydrofolate Reductase From Mycobacteri1.5.1.32.6e-1540.8103 &W&D--
3q1hADihydrofolate Reductase From Yersinia Pe5.8e-1429.9154 &W&D&T
2d0kA, 2d0kBMethionine-Free Mutant Of Escherichia Co1.5.1.31.2e-1230.9152 &W&D&T
1ddsA, 1ddsB, 1ddrA, 1ddrB, 3dauA, 3k74A, 4eigA, 4eizA, 4eizB, 4ej1A, 4ej1B, 4fhbAMolecule: Dihydrofolate Reductase (E.C.11.5.1.33.6e-1229.6152 &W&D&T
1dhjA, 1dhjBLong-Range Structural Effects In A Secon1.5.1.34.3e-1229.6152 &W&S&T
3drcA, 3drcB, 1dyhA, 1dyhB, 1dyiA, 1dyiB, 1dyjA, 1dyjB, 1rb2A, 1rb2B, 1rb3A, 1rb3B, 1rd7A, 1rd7B, 1re7A, 1re7B, 1jolA, 1jolB, 2anoA, 2anqA, 2inqA, 1dreA, 1drhA, 1jomA, 1ra1A, 1ra2A, 1ra3A, 1ra8A, 1ra9A, 1rc4A, 1rf7A, 1rg7A, 1rh3A, 1rx1A, 1rx2A, 1rx3A, 1rx4A, 1rx5A, 1rx6A, 1rx7A, 1rx8A, 1rx9A, 5dfrA, 6dfrA, 7dfrA, 3kfyA, 3ochA, 3ochB, 3ql3A, 3qylA, 3qyoA, 3r33AInvestigation Of The Functional Role Of 1.5.1.34.3e-1229.6152 &W&D&T
2inqBNeutron Escherichia Coli Dihydrofolate R1.5.1.36.2e-1230.6144 &W&D&T
4dfrA, 4dfrB, 1tdrA, 1tdrBCrystal Structures Of Escherichia Coli A1.5.1.36.2e-1230.6144 &W&D&T
1draA, 1draBUnliganded Escherichia Coli Dihydrofolat1.5.1.31.3e-1128.9152 &W&E&T
1dhiA, 1dhiBLong-Range Structural Effects In A Secon1.5.1.31.8e-1128.9152 &W&S&T
1drbA, 1drbBUnliganded Escherichia Coli Dihydrofolat1.5.1.33.8e-1128.9152 &W&C&T
2drcA, 2drcBInvestigation Of The Functional Role Of 1.5.1.35.4e-1128.9152 &F&D&T
3ql0AN23ppS148A MUTANT OF E. COLI DIHYDROFOLA5.4e-1128.9152 &W&D&T
2jybA, 2ithABinary Hvdhfr1:folate Complex1.5.1.35.5e-1133.3132 &W&D&S
1vdrA, 1vdrBDihydrofolate Reductase1.5.1.36.6e-1133.3132 &W&D&S
1ai9A, 1ai9B, 1aoeA, 1aoeB, 1ia1A, 1ia1B, 1ia2A, 1ia2B, 1ia3A, 1ia3B, 1ia4A, 1ia4B, 1m78A, 1m78B, 1m79A, 1m79B, 1m7aA, 1m7aB, 3qlrA, 3qlrB, 3qlsA, 3qlsB, 3qlwA, 3qlwBCandida Albicans Dihydrofolate Reductase1.5.1.37.6e-0928.6175 &W&E&T
1dr1A, 1dr2A, 1dr3A, 1dr4A, 1dr5A, 1dr6A, 1dr7A, 8dfrA2.2 Angstroms Chicken Liver Dihydrofolat1.5.1.31.8e-0828.2174 &W&E&T
2fzjA, 3d80A, 3d84X, 3k47ANew Insights Into Dhfr Interactions: Ana1.5.1.32.7e-0729.6186 &W&E&T
3ro9A, 3ro9B, 3roaA, 3roaBCandida Glabrata Dihydrofolate Reductase2.9e-0729.8124 &W&E&T
3cseA, 3cseB, 3eejA, 3eejB, 3eekA, 3eekB, 3eelA, 3eelB, 3eemA, 3eemB, 3qlxA, 3qlxB, 3qlyA, 3qlyB, 3qlzA, 3qlzBCandida Glabrata Dihydrofolate Reductase2.9e-0729.8124 &W&E&T
3k45AAlternate Binding Modes Observed For The1.5.1.33.2e-0729.0186 &W&E&T
3i3rA, 3i3rB, 3k2hA, 3k2hB, 3kjrA, 3kjrBX-Ray Structure Dihydrofolate ReductaseT7.2e-0724.0171 &W&D&T
3nrrA, 3nrrBCo-Dihydrofolate Reductase-Thymidylate S7.2e-0724.0171 &W&D&T
1u70AUnderstanding The Role Of Leu22 Variants1.5.1.31.2e-0629.0186 &W&E&T
2oipA, 2oipB, 2oipC, 2oipD, 2oipEThe S290g Active Site Mutant Of Ts- Dhfr1.5e-0627.6163 &W&D&T
1qzfA, 1qzfB, 1qzfC, 1qzfD, 1qzfE, 1sejA, 1sejB, 1sejC, 1sejD, 1sejEDhfr-Ts From Cryptosporidium Hominis1.5e-0627.6163 &W&D&T
3dl6A, 3dl6B, 3dl6C, 3dl6D, 3dl6EThe A287fS290G ACTIVE SITE MUTANT OF Ts-1.5e-0627.6163 &W&D&T
3dl5A, 3dl5B, 3dl5C, 3dl5D, 3dl5EThe A287f Active Site Mutant Of Ts- Dhfr1.5e-0627.6163 &W&D&T
3hj3A, 3hj3B, 3hj3C, 3hj3DThe Chts-Dhfr F207a Non-Active Site Mut1.5e-0627.6163 &W&D&T
3l3rAStructural, Computational And Kinetic Da1.5.1.35.9e-0631.9141 &W&E&T
3ghvA, 3s3vAHuman Dihydrofolate Reductase Q35kN64F D1.5.1.35.9e-0631.9141 &W&E&T
3f8yA, 3gi2ACorrelations Of Human Dihydrofolate Redu1.5.1.35.9e-0631.9141 &W&E&T
3nxoAPerferential Selection Of Isomer Binding1.5.1.38.4e-0631.9141 &W&E&T
1dhfA, 1dhfB, 2dhfA, 2dhfB, 1kmsA, 1kmvA, 1pd8A, 1pd9A, 1pdbA, 1s3uA, 1s3vA, 1s3wA, 1u72A, 1yhoA, 2c2sA, 2c2sB, 2c2tA, 2c2tB, 1drfA, 1hfrA, 1ohjA, 1ohkA, 3ghwA, 3nxrA, 3nxtA, 3nxvA, 3nxxA, 3nxyA, 3nzdA, 3ntzA, 3nu0A, 3s7aA, 4ddrACrystal Structures Of Recombinant Human 1.5.1.38.4e-0631.9141 &W&E&T
1mvsA, 1mvtA, 3fs6A, 3gyfA, 2w3aA, 2w3aB, 2w3bA, 2w3bB, 2w3mA, 2w3mBAnalysis Of Two Polymorphic Forms Of A P1.5.1.38.5e-0631.9141 &W&E&T
3ghcADesign, Synthesis, And X-Ray Classical A1.5.1.31.2e-0531.9141 &W&E&T
3oafA, 3n0hAStructural And Kinetic Data For Antifola1.5.1.31.2e-0531.9141 &W&E&T
3f8zAHuman Dihydrofolate Reductase Structural1.5.1.31.2e-0531.9141 &W&E&T
3f91AStructural Data For Human Active Site Mu1.5.1.31.2e-0531.9141 &W&E&T
1dlrAMethotrexate-Resistant Variants Of Human1.5.1.31.7e-0531.2141 &W&E&T
1hfqAComparison Of Ternary Crystal Complexes 1.5.1.31.7e-0531.9141 &W&E&T
1bozA, 1hfpAStructure-Based Design And Synthesis Of 1.5.1.32.1e-0531.9141 &W&E&T
3eigAA Methotrexate-Resistant Mutant Of Human1.5.1.32.1e-0531.9141 &W&E&T
1dlsAMethotrexate-Resistant Variants Of Human1.5.1.32.5e-0531.2141 &W&E&T
3rg9A, 3rg9BTrypanosoma Brucei Dihydrofolate Reducta1.5.1.3, 2.1.1.452.9e-0539.773 &W&D--
3qfxA, 3qfxBTrypanosoma Brucei Dihydrofolate Reducta1.5.1.3, 2.1.1.452.9e-0539.773 &W&D--
1cz3A, 1cz3B, 1d1gA, 1d1gBDihydrofolate Reductase From Thermotoga 1.5.1.33.1e-0532.9140 &W&D&T
2bl9A, 2blbAX-Ray Plasmodium Vivax Dihydrofolate Red1.5.1.3, 2.1.1.453.4e-0525.0136 ----&T
1u71AUnderstanding The Role Of Leu22 Variants1.5.1.33.6e-0531.2141 &W&E&T
2blaA, 2blcASp21 Double Mutant P. Vivax Dihydrofolat1.5.1.3, 2.1.1.454.9e-0525.0136 ----&T
1vj3AStructural Studies On Bio-Active Compoun1.5.1.35.8e-0526.9145 &W&E&T
1cd2A, 2cd2A, 3cd2A, 4cd2A, 1e26A, 1ly3A, 1ly4A, 1klkA, 1s3yA, 2fzhA, 2fziA, 1dajA, 1dyrA, 3nz6X, 3nz9X, 3nzaX, 3nzbX, 3nzcX, 3td8ALigand Induced Conformational Changes In1.5.1.35.9e-0526.9145 &W&E&T
1j3iA, 1j3iB, 3dgaA, 3dgaBWild-Type Plasmodium Falciparum Dihydrof1.5.1.3, 2.1.1.450.0002622.8136 ----&T
1j3jA, 1j3jBDouble Mutant (C59r+s108n) Plasmodium Fa1.5.1.3, 2.1.1.450.0003722.8136 ----&T
3invA, 3invB, 3irmA, 3irmB, 3irmC, 3irmD, 3irnA, 3irnB, 3irnC, 3irnD, 3iroA, 3iroB, 3iroC, 3iroDTrypanosoma Cruzi Dihydrofolate Reductas1.5.1.3, 2.1.1.450.0004138.473 &W&D--
3um5A, 3um5B, 3um6A, 3um6BDouble Mutant (A16v+s108t) Plasmodium Fa0.0004223.5136 ----&T
1j3kA, 1j3kB, 3dg8A, 3dg8BQuadruple Mutant (n51i+c59r+s108n+i164l)1.5.1.3, 2.1.1.450.0004522.8136 ----&T
2h2qA, 2h2qB, 3cl9A, 3clbA, 3clbB, 3clbC, 3clbD, 3hbbA, 3hbbB, 3hbbC, 3hbbD, 3kjsA, 3kjsB, 3kjsC, 3kjsDTrypanosoma Cruzi Dihydrofolate Reductas1.5.1.3, 2.1.1.450.0007138.473 &W&D--
3qgtA, 3qgtB, 3um8A, 3um8B, 4dpdA, 4dpdBWild-Type Pfdhfr-Ts Complexed With Nadph0.0007222.8136 ----&T

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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