Structure of PDB 4pel Chain H

Receptor sequence
>4pelH (length=557) Species: 580 (Kluyvera cryocrescens) [Search protein sequence]
CNMWVIGKNKAQDAKAIMVNGPQFGWYAPAYTYGIGLHGAGYDVTGNTPF
AYPGLVFGHNGTISWGSTAGFGDDVDIFAEKLSAEKPGYYQHNGEWVKML
SRKETIAVKDGQPETFTVWRTLHGNVIKTDTATQTAYAKARAWDGKEVAS
LLAWTHQMKAKNWPEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQ
PGHDPRLPVPGTGKWDWKGLLSFDLNPKVYNPQSGYIANWNNSPQKDYPA
SDLFAFLWGGADRVTEIDTTLDKQPRFTADQAWDVIRQTSRRDLNLRLFL
PALKDATANLAENDPRRQLVDKLASWDGENLVNDDGKTYQQPGSAILNAW
LTSMLKRTVVAAVPAPFGKWYSASGYETTQDGPTGSLNISVGAKILYEAL
QGDKSPIPQAVDLFGGKPQQEVILAALDDAWQTLSKRYGNDVTGWKTPAM
ALTFRANNFFGVPQAAAKEARHQAEYQNRGTENDMIVFSPTSGNRPVLAW
DVVAPGQSGFIAPDGKADKHYDDQLIMYESFGRKSLWLTPQDVDEHKESQ
EVLQVQR
3D structure
PDB4pel Penicillin G acylase
ChainH
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C1 A69 N241
Catalytic site (residue number reindexed from 1) C1 A69 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 H D73 V75 D76 P205 D252 D73 V75 D76 P205 D252
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Biological Process
GO:0017000 antibiotic biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4pel, PDBe:4pel, PDBj:4pel
PDBsum4pel
PubMed
UniProtA0A068F6N5

[Back to BioLiP]