Structure of PDB 3gzy Chain A

Receptor sequence
>3gzyA (length=440) Species: 285 (Comamonas testosteroni) [Search protein sequence]
NWTPDAIRALVDQDNGKLDARIYADQDLYQLELERVFGRSWLMLGHETHI
PKIGDYLTTYMGEDPVIMVRQKDQSIKVFLNQCRHRGMRIVRSDGGNAKA
FTCTYHGWAYDIAGNLVNVPFEKEAFCDKKEGDCGFDKADWGPLQARVET
YKGLVFANWDPEAPDLKTYLSDAMPYMDVMLDRTEAGTEAIGGIQKWVIP
CNWKFAAEQFCSDMYHAGTMSHLSGVLAGLPPEMDLTQIQLSKNGNQFRS
AWGGHGAGWFINDSSILLSVVGPKITQYWTQGPAAEKAARRVPQLPILDM
FGQHMTVFPTCSFLPGINTIRTWHPRGPNEVEVWAFVLVDADAPEDIKEE
FRLQNIRTFNAGGVFEQDDGENWVEIQRVMRGHKAKSTSLCAKMGLNVPN
KNNPAYPGKTAYVYAEEAARGMYHHWSRMMSEPSWDTLKP
3D structure
PDB3gzy Structural Characterization of Pandoraea pnomenusa B-356 Biphenyl Dioxygenase Reveals Features of Potent Polychlorinated Biphenyl-Degrading Enzymes
ChainA
Resolution1.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H123 D230 H233 H239 D386
Catalytic site (residue number reindexed from 1) H106 D213 H216 H222 D369
Enzyme Commision number 1.14.12.18: biphenyl 2,3-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 FE2 A Q226 H233 H239 D386 Q209 H216 H222 D369
BS02 FES A C100 H102 R103 C120 Y122 H123 W125 C83 H85 R86 C103 Y105 H106 W108
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0018687 biphenyl 2,3-dioxygenase activity
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:3gzy, PDBe:3gzy, PDBj:3gzy
PDBsum3gzy
PubMed23308114
UniProtQ46372|BPHA_COMTE Biphenyl dioxygenase subunit alpha (Gene Name=bphA)

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