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5LS3

Crystal structure of metallo-beta-lactamase SPM-1 with Y58C mutation

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
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS108
BHIS110
BHIS197
BZN402
BHOH566

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN B 402
ChainResidue
BHOH566
BHOH638
BASP112
BCYS216
BHIS258
BZN401

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 403
ChainResidue
AHIS33
AASP35
BHIS33
BASP35

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AASP112
ACYS216
AHIS258
AZN402
AHOH586

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS108
AHIS110
AHIS197
AZN401
AHOH586

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkkkLLfGgCMIK
ChainResidueDetails
BPRO207-LYS219

220113

PDB entries from 2024-05-22

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