Structure of PDB 2ckf Chain A

Receptor sequence
>2ckfA (length=448) Species: 279135 (Sphingomonas sp. CHY-1) [Search protein sequence]
MSGDTTLVDTVNASQSRQVFWDRDVYDLEIERIFSRAWLMLGHKSLLPKP
GDFITTYMAEDKIILSHQSDGTFRAFINSCTHRGNQICHADSGNAKAFVC
NYHGWVYGQDGSLVDVPLESRCYHNKLDKQELAAKSVRVETYKGFIFGCH
DPEAPSLEDYLGEFRFYLDTIWEGGGAGLELLGPPMKSLLHCNWKVPVEN
FVGDGYHVGWTHAAALGQIGGPLAGLAGNRADDLGLQFTTRHGHGFGVID
NAAAAIHRKGDGWNKYLEDTRGEVRRKFGADRERLYVGHWNGAIFPNCSF
LYGTNTFKIWHPRGPHEIEVWTYTMVPSDADPATKSAIQREATRTFGTAG
TLESDDGENMSSATYVNRGVITRDGMMNSTMGVGYEGPHPVYPGIVGISF
IGETSYRGFYRFWKEMIDAPDWASVKANDDNWDSVFTNRNFWNEKLNA
3D structure
PDB2ckf The Catalytic Pocket of the Ring-Hydroxylating Dioxygenase from Sphingomonas Chy-1.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H103 D204 H207 H212 D360
Catalytic site (residue number reindexed from 1) H103 D204 H207 H212 D356
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 FES A C80 H82 R83 C100 Y102 H103 W105 C80 H82 R83 C100 Y102 H103 W105
BS02 FE A H207 H212 D360 H207 H212 D356
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0044237 cellular metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2ckf, PDBe:2ckf, PDBj:2ckf
PDBsum2ckf
PubMed17157819
UniProtQ65AT1

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