Structure of PDB 3u52 Chain B

Receptor sequence
>3u52B (length=493) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence]
KKLNLKDKYQYLTRDMAWEPTYQDKKDIFPEEDFEGIKITDWSQWEDPFR
LTMDAYWKYQAEKEKKLYAIFDAFAQNNGHQNISDARYVNALKLFISGIS
PLEHAAFQGYSKVGRQFSGAGARVACQMQAIDELRHSQTQQHAMSHYNKH
FNGLHDGPHMHDRVWYLSVPKSFFDDARSAGPFEFLTAISFSFEYVLTNL
LFVPFMSGAAYNGDMATVTFGFSAQSDEARHMTLGLEVIKFILEQHEDNV
PIVQRWIDKWFWRGFRLLSLVSMMMDYMLPNKVMSWSEAWEVYYEQNGGA
LFKDLERYGIRPPKYQDVANDAKHHLSHQLWTTFYQYCQATNFHTWIPEK
EEMDWMSEKYPDTFDKYYRPRYEYLAKEAAAGRRFYNNTLPQLCQVCQIP
TIFTEKDAPTMLSHRQIEHEGERYHFCSDGCCDIFKHEPEKYIQAWLPVH
QIYQGNCEGGDLETVVQKYYHINIGEDNFDYVGSPDQKHWLSI
3D structure
PDB3u52 Analysis of Substrate Access to Active Sites in Bacterial Multicomponent Monooxygenase Hydroxylases: X-ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase from Pseudomonas sp. OX1.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E108 E138 H141 E199 E233 H236
Catalytic site (residue number reindexed from 1) E103 E133 H136 E194 E228 H231
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 FE B E108 E138 H141 E103 E133 H136
BS02 FE B E199 E233 H236 E194 E228 H231
BS03 ZN B C399 C402 C436 C394 C397 C431
BS04 CU B H155 H494 H150 H489
BS05 GOL B L107 E108 A111 E138 I194 F198 L102 E103 A106 E133 I189 F193
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3u52, PDBe:3u52, PDBj:3u52
PDBsum3u52
PubMed22136180
UniProtQ84AQ2

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