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UniProt P00469

P00469

P00469 (UniProt P00469): 103 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P00469
Experimental structures
103
Predicted models
0

Structures

103 records of P00469 in the MolNFT archive: 103 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1BO7Thymidylate synthase R179T mutantx-ray diffractionA——
1BO7Thymidylate synthase R179T mutantx-ray diffractionA——
1BO8Thymidylate synthase R178T mutantx-ray diffractionA——
1BO8Thymidylate synthase R178T mutantx-ray diffractionA——
1BP0Thymidylate synthase R23I mutantx-ray diffractionA——
1BP0Thymidylate synthase R23I mutantx-ray diffractionA——
1BP6Thymidylate synthase R23I, R179T double mutantx-ray diffractionA——
1BP6Thymidylate synthase R23I, R179T double mutantx-ray diffractionA——
1BPJThymidylate synthase R178T, R179T double mutantx-ray diffractionA——
1BPJThymidylate synthase R178T, R179T double mutantx-ray diffractionA——
1JMFContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1JMFContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——
1JMGContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1JMGContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——
1JMHContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1JMHContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——
1JMIContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1JMIContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——
1LCALactobacillus casei thymidylate synthase ternary complex with dump and CB3717x-ray diffractionA——
1LCALactobacillus casei thymidylate synthase ternary complex with dump and CB3717x-ray diffractionA——
1LCBLactobacillus casei thymidylate synthase ternary complex with dtmp and H2FOLATEx-ray diffractionA——
1LCBLactobacillus casei thymidylate synthase ternary complex with dtmp and H2FOLATEx-ray diffractionA——
1LCELactobacillus casei thymidylate synthase ternary complex with dump and CH2THFx-ray diffractionA——
1LCELactobacillus casei thymidylate synthase ternary complex with dump and CH2THFx-ray diffractionA——
1NJAThymidylate synthase, mutation, N229C with 2'-deoxycytidine 5'-monophosphate (dcmp)x-ray diffractionA——
1NJAThymidylate synthase, mutation, N229C with 2'-deoxycytidine 5'- monophosphate (dcmp)x-ray diffractionA——
1NJBThymidylate synthasex-ray diffractionA——
1NJBThymidylate synthasex-ray diffractionA——
1NJCThymidylate synthase, mutation, N229D with 2'-deoxycytidine 5'-monophosphate (dcmp)x-ray diffractionA——
1NJCThymidylate synthase, mutation, N229D with 2'-deoxycytidine 5'- monophosphate (dcmp)x-ray diffractionA——
1NJDThymidylate synthase, mutation, N229D with 2'-deoxyuridine 5'-monophosphate (dump)x-ray diffractionA——
1NJDThymidylate synthase, mutation, N229D with 2'-deoxyuridine 5'- monophosphate (dump)x-ray diffractionA——
1NJEThymidylate synthase with 2'-deoxycytidine 5'-monophosphate (dcmp)x-ray diffractionA——
1NJEThymidylate synthase with 2'-deoxycytidine 5'-monophosphate (dcmp)x-ray diffractionA——
1TDAStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1TDAStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1TDBStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1TDBStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1TDCStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1TDCStructures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment…x-ray diffractionA——
1THYRefined structures of substrate-bound and phosphate-bound thymidylate synthase from lactobacillus…x-ray diffractionA——
1THYRefined structures of substrate-bound and phosphate-bound thymidylate synthase from lactobacillus…x-ray diffractionA——
1TSLL. casei thymidylate synthase with species specific inhibitorx-ray diffractionA——
1TSLL. casei thymidylate synthase with species specific inhibitorx-ray diffractionA——
1TSML. casei thymidylate synthase with species specific inhibitorx-ray diffractionA——
1TSML. casei thymidylate synthase with species specific inhibitorx-ray diffractionA——
1TSVThymidylate synthase R179A mutantx-ray diffractionA——
1TSVThymidylate synthase R179A mutantx-ray diffractionA——
1TSWThymidylate synthase R179A mutantx-ray diffractionA——
1TSWThymidylate synthase R179A mutantx-ray diffractionA——
1TSXThymidylate synthase R179E mutantx-ray diffractionA——
1TSXThymidylate synthase R179E mutantx-ray diffractionA——
1TSYThymidylate synthase R179K mutantx-ray diffractionA——
1TSYThymidylate synthase R179K mutantx-ray diffractionA——
1TSZThymidylate synthase R179K mutantx-ray diffractionA——
1TSZThymidylate synthase R179K mutantx-ray diffractionA——
1TVUContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1TVUContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——
1TVVContributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of thymidylate…x-ray diffractionA——
1TVVContributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate…x-ray diffractionA——

43 records more on the page itself.

Elsewhere

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