Structure of PDB 1eir Chain A

Receptor sequence
>1eirA (length=289) Species: 307 (Pseudomonas sp. KKS102) [Search protein sequence]
SIERLGYLGFAVKDVPAWDHFLTKSVGLMAAGSAGDAALYRADQRAWRIA
VQPGELDDLAYAGLEVDDAAALERMADKLRQAGVAFTRGDEALMQQRKVM
GLLCLQDPFGLPLEIYYGPAEIFHEPFLPSAPVSGFVTGDQGIGHFVRCV
PDTAKAMAFYTEVLGFVLSDIIDIQMGPETSVPAHFLHCNGRHHTIALAA
FPIPKRIHHFMLQANTIDDVGYAFDRLDAAGRITSLLGRHTNDQTLSFYA
DTPSPMIEVEFGWGPRTVDSSWTVARHSRTAMWGHKSVR
3D structure
PDB1eir Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.39: biphenyl-2,3-diol 1,2-dioxygenase.
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 H145 H209 E260 H145 H209 E260
BS02 BPY A F186 H194 F201 H209 H240 N242 Y249 T280 F186 H194 F201 H209 H240 N242 Y249 T280
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005506 iron ion binding
GO:0008198 ferrous iron binding
GO:0018583 biphenyl-2,3-diol 1,2-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0042178 xenobiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1eir, PDBe:1eir, PDBj:1eir
PDBsum1eir
PubMed11293547
UniProtP17297|BPHC_PSES1 Biphenyl-2,3-diol 1,2-dioxygenase (Gene Name=bphC)

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