Structure of PDB 1cp9 Chain B

Receptor sequence
>1cp9B (length=553) Species: 587 (Providencia rettgeri) [Search protein sequence]
SNVWLVGKTKASGAKAILLNGPQFGWFNPAYTYGIGLHGAGFNIVGNTPF
AYPAILFGHNGHVSWGSTAGFGDGVDIFAEQVSPEDPNSYLHQGQWKKML
SRQETLNVKGEQPITFEIYRTVHGNVVKRDKTTHTAYSKARAWDGKELTS
LMAWVKQGQAQNWQQWLDQAQNQALTINWYYADKDGNIGYVHTGHYPDRQ
INHDPRLPVSGTGEWDWKGIQPFANNPKVYNPKSGYIANWNNSPAKNYPA
SDLFAFLWGSADRVKEIDNRIEAYDKLTADDMWAILQQTSRVDLNHRLFT
PFLTQATQGLPSNDNSVKLVSMLQQWDGINQLSSDGKHYIHPGSAILDIW
LKEMLKATLGQTVPAPFDKWYLASGYETTQEGPTGSLNISTGAKLLYESL
LEDKSPISQSIDLFSGQPQNDVIRKTLNTTYQKMIEKYGDNPANWQTPAT
ALTFRENNFFGIPQALPQENFHQNEYHNRGTENDLIVFTEEGVSAWDVVA
PGQSGFISPQGKPSPHYQDQLSLYQQFGKKPLWLNSEDVAPYIESTETLI
IER
3D structure
PDB1cp9 Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1 Q23 A69 N241 N483
Catalytic site (residue number reindexed from 1) S1 Q23 A69 N241 N483
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA B D73 V75 D76 P205 D252 D73 V75 D76 P205 D252
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1cp9, PDBe:1cp9, PDBj:1cp9
PDBsum1cp9
PubMed10548042
UniProtQ7WZI9

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