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5EVK

Crystal structure of the metallo-beta-lactamase L1 in complex with the bisthiazolidine inhibitor L-CS319

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 3C7 A 401
ChainResidue
ATYR33
AHOH501
AHIS116
AASP120
AHIS121
AHIS196
ASER225
AHIS263
AZN403
AZN404

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AARG172
AVAL179
AILE180
ATHR181
AHOH713

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
AASP120
AHIS121
AHIS263
A3C7401

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 404
ChainResidue
AHIS116
AHIS118
AHIS196
A3C7401

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues21
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG
ChainResidueDetails
ALEU113-GLY133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:17999929, ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS116
AHIS118
AASP120
AHIS121
AHIS196

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASP220

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811546
ChainResidueDetails
AHIS263

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120metal ligand
AHIS121metal ligand
AHIS196metal ligand
ATYR229electrostatic stabiliser, hydrogen bond donor
AHIS263metal ligand

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PDB entries from 2024-07-24

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