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4S2M

Crystal Structure of OXA-163 complexed with iodide in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
C0005886cellular_componentplasma membrane
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
D0005886cellular_componentplasma membrane
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 301
ChainResidue
ATRP157

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 302
ChainResidue
AARG206
DARG206

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 303
ChainResidue
AARG186

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 304
ChainResidue
AASN48
ALYS51
CLYS51

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 305
ChainResidue
AASN32

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 306
ChainResidue
ALEU67

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 307
ChainResidue
ALYS180

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 301
ChainResidue
BARG206
CARG206

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 302
ChainResidue
BTRP157

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 303
ChainResidue
BLEU67

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD C 304
ChainResidue
CLEU67

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD D 301
ChainResidue
DTRP157

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD D 303
ChainResidue
DHIS178
DLYS180

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD D 304
ChainResidue
DLEU67

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD D 305
ChainResidue
DGLN41
DGLY42

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL
ChainResidueDetails
APRO68-LEU78

239149

PDB entries from 2025-07-23

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