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1H8Z

Crystal structure of the class D beta-lactamase OXA-13

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1267
ChainResidue
ASER67
ATHR206
AGLY207
AARG250
AHOH2027
AHOH2089
AHOH2112
AHOH2113

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1268
ChainResidue
ALYS182
AHOH2070
BASN85
BGLU86
AASN176

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B1267
ChainResidue
BSER67
BTHR206
BGLY207
BPHE208
BARG250
BHOH2084

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1268
ChainResidue
AASN85
AGLU86
BASN176
BLYS182

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1269
ChainResidue
BLEU247
BARG250
BLYS251
BHOH2099

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPsAI
ChainResidueDetails
APRO65-ILE75

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
ASER67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
BSER67

225158

PDB entries from 2024-09-18

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