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1CP9

CRYSTAL STRUCTURE OF PENICILLIN G ACYLASE FROM THE BRO1 MUTANT STRAIN OF PROVIDENCIA RETTGERI

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0017000biological_processantibiotic biosynthetic process
B0016787molecular_functionhydrolase activity
B0017000biological_processantibiotic biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 554
ChainResidue
BASP252
AGLU150
BASP73
BVAL75
BASP76
BPRO205

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 555
ChainResidue
BLYS98
BARG270
BGLN288
BHOH775

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 255
ChainResidue
APCA1
ASER2
ATHR3
AGLN4
AASN20
AHOH828
AHOH830

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 269
ChainResidue
ATHR128
APHE130
BGLU491
BSER494
BHOH981

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 556
ChainResidue
BGLN200
BASN441
BASN444
BHOH1038

site_idAS
Number of Residues4
DetailsSER B 1 IS THE CATALYTIC RESIDUE GLN B 23, ALA B 69 AND ASN B 241 FORM AN OXYANION HOLE
ChainResidue
BSER1
BGLN23
BALA69
BASN241

220113

PDB entries from 2024-05-22

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