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1SML

METALLO BETA LACTAMASE L1 FROM STENOTROPHOMONAS MALTOPHILIA

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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 270
ChainResidue
AASP88
AHIS89
AHIS225
AZN271
AHOH528
AHOH568

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 271
ChainResidue
AZN270
AHOH528
AHOH568
AHIS84
AHIS86
AHIS160

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues21
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG
ChainResidueDetails
ALEU81-GLY101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10433708, 9811546
ChainResidueDetails
ATYR191

site_idMCSA1
Number of Residues7
DetailsM-CSA 258
ChainResidueDetails
AHIS84metal ligand
AHIS86metal ligand
AASP88metal ligand
AHIS89metal ligand
AHIS160metal ligand
ATYR191electrostatic stabiliser, hydrogen bond donor
AHIS225metal ligand

245663

PDB entries from 2025-12-03

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