Structure of PDB 2inn Chain A

Receptor sequence
>2innA (length=496) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence]
KNKKLNLKDKYQYLTRDMAWEPTYQDKKDIFPEEDFEGIKITDWSQWEDP
FRLTMDAYWKYQAEKEKKLYAIFDAFAQNNGHQNISDARYVNALKLFISG
ISPLEHAAFQGYSKVGRQFSGAGARVACQMQAIDELRHSQTQQHAMSHYN
KHFNGLHDGPHMHDRVWYLSVPKSFFDDARSAGPFEFLTAISFSFEYVLT
NLLFVPFMSGAAYNGDMATVTFGFSAQSDEARHMTLGLEVIKFILEQHED
NVPIVQRWIDKWFWRGFRLLSLVSMMMDYMLPNKVMSWSEAWEVYYEQNG
GALFKDLERYGIRPPKYQDVANDAKHHLSHQLWTTFYQYCQATNFHTWIP
EKEEMDWMSEKYPDTFDKYYRPRYEYLAKEAAAGRRFYNNTLPQLCQVCQ
IPTIFTEKDAPTMLSHRQIEHEGERYHFCSDGCCDIFKHEPEKYIQAWLP
VHQIYQGNCEGGDLETVVQKYYHINIGEDNFDYVGSPDQKHWLSIK
3D structure
PDB2inn X-ray Structure of a Hydroxylase-Regulatory Protein Complex from a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas sp. OX1 Phenol Hydroxylase.
ChainA
Resolution2.7 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) E105 E135 H138 E196 E230 H233
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 A E138 E199 E233 H236 E135 E196 E230 H233
BS02 FE A E108 E138 H141 E105 E135 H138
BS03 ZN A C399 C402 C432 C436 C396 C399 C429 C433
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:2inn, PDBe:2inn, PDBj:2inn
PDBsum2inn
PubMed17176061
UniProtQ84AQ2

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