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7PGO

Crystal Structure of a Class D Carbapenemase_R250A

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0005886cellular_componentplasma membrane
AAA0008658molecular_functionpenicillin binding
AAA0008800molecular_functionbeta-lactamase activity
AAA0016787molecular_functionhydrolase activity
AAA0017001biological_processantibiotic catabolic process
AAA0046677biological_processresponse to antibiotic
AAA0071555biological_processcell wall organization
BBB0005886cellular_componentplasma membrane
BBB0008658molecular_functionpenicillin binding
BBB0008800molecular_functionbeta-lactamase activity
BBB0016787molecular_functionhydrolase activity
BBB0017001biological_processantibiotic catabolic process
BBB0046677biological_processresponse to antibiotic
BBB0071555biological_processcell wall organization
CCC0005886cellular_componentplasma membrane
CCC0008658molecular_functionpenicillin binding
CCC0008800molecular_functionbeta-lactamase activity
CCC0016787molecular_functionhydrolase activity
CCC0017001biological_processantibiotic catabolic process
CCC0046677biological_processresponse to antibiotic
CCC0071555biological_processcell wall organization
DDD0005886cellular_componentplasma membrane
DDD0008658molecular_functionpenicillin binding
DDD0008800molecular_functionbeta-lactamase activity
DDD0016787molecular_functionhydrolase activity
DDD0017001biological_processantibiotic catabolic process
DDD0046677biological_processresponse to antibiotic
DDD0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL
ChainResidueDetails
AAAPRO68-LEU78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:25406838, ECO:0000269|PubMed:26731698, ECO:0000269|PubMed:31358584, ECO:0000269|PubMed:32150407, ECO:0007744|PDB:4WMC, ECO:0007744|PDB:5FAQ, ECO:0007744|PDB:5FAS, ECO:0007744|PDB:6P97, ECO:0007744|PDB:6P98, ECO:0007744|PDB:6P99, ECO:0007744|PDB:6P9C, ECO:0007744|PDB:6V1O
ChainResidueDetails
AAASER70
BBBSER70
CCCSER70
DDDSER70

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8RLA6
ChainResidueDetails
AAASER70
DDDSER70
DDDSER118
DDDALA250
AAASER118
AAAALA250
BBBSER70
BBBSER118
BBBALA250
CCCSER70
CCCSER118
CCCALA250

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13661
ChainResidueDetails
AAAKCX73
BBBKCX73
CCCKCX73
DDDKCX73

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|PIRSR:PIRSR602137-50, ECO:0000269|PubMed:19477418, ECO:0000269|PubMed:25406838, ECO:0007744|PDB:3HBR, ECO:0007744|PDB:4WMC
ChainResidueDetails
AAAKCX73
BBBKCX73
CCCKCX73
DDDKCX73

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PDB entries from 2025-06-18

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