Structure of PDB 2inp Chain A

Receptor sequence
>2inpA (length=494) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence]
KKLNLKDKYQYLTRDMAWEPTYQDKKDIFPEEDFEGIKITDWSQWEDPFR
LTMDAYWKYQAEKEKKLYAIFDAFAQNNGHQNISDARYVNALKLFISGIS
PLEHAAFQGYSKVGRQFSGAGARVACQMQAIDELRHSQTQQHAMSHYNKH
FNGLHDGPHMHDRVWYLSVPKSFFDDARSAGPFEFLTAISFSFEYVLTNL
LFVPFMSGAAYNGDMATVTFGFSAQSDEARHMTLGLEVIKFILEQHEDNV
PIVQRWIDKWFWRGFRLLSLVSMMMDYMLPNKVMSWSEAWEVYYEQNGGA
LFKDLERYGIRPPKYQDVANDAKHHLSHQLWTTFYQYCQATNFHTWIPEK
EEMDWMSEKYPDTFDKYYRPRYEYLAKEAAAGRRFYNNTLPQLCQVCQIP
TIFTEKDAPTMLSHRQIEHEGERYHFCSDGCCDIFKHEPEKYIQAWLPVH
QIYQGNCEGGDLETVVQKYYHINIGEDNFDYVGSPDQKHWLSIK
3D structure
PDB2inp X-ray Structure of a Hydroxylase-Regulatory Protein Complex from a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas sp. OX1 Phenol Hydroxylase.
ChainA
Resolution2.3 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 A E138 E199 E233 H236 E133 E194 E228 H231
BS02 ZN A C399 C402 C432 C436 C394 C397 C427 C431
BS03 FE A E108 E138 H141 E103 E133 H136
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:2inp, PDBe:2inp, PDBj:2inp
PDBsum2inp
PubMed17176061
UniProtQ84AQ2

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