Structure of PDB 1ai7 Chain B

Receptor sequence
>1ai7B (length=557) Species: 562 (Escherichia coli) [Search protein sequence]
SNMWVIGKSKAQDAKAIMVNGPQFGWYAPAYTYGIGLHGAGYDVTGNTPF
AYPGLVFGHNGVISWGSTAGFGDDVDIFAERLSAEKPGYYLHNGKWVKML
SREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVAS
LLAWTHQMKAKNWQQWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQ
SGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANWNNSPQKDYPA
SDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFL
PTLQAATSGLTQSDPRRQLVETLTRWDGINLLNDDGKTWQQPGSAILNVW
LTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAV
QGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAM
ALTFRANNFFGVPQAAAEETRHQAEYQNRGTENDMIVFSPTTSDRPVLAW
DVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQ
EVLHVQR
3D structure
PDB1ai7 Ligand-induced conformational change in penicillin acylase.
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 F71 N241
Catalytic site (residue number reindexed from 1) S1 Q23 A69 F71 N241
Enzyme Commision number 3.5.1.11: penicillin amidase.
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:1ai7, PDBe:1ai7, PDBj:1ai7
PDBsum1ai7
PubMed9813130
UniProtP06875|PAC_ECOLX Penicillin G acylase (Gene Name=pac)

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