Structure of PDB 2b1x Chain A

Receptor sequence
>2b1xA (length=441) [Search protein sequence]
MLSNELRQTLQKGLHDVNSDWTVPAAIINDPEVHDVERERIFGHAWVFLA
HESEIPERGDYVVRYISEDQFIVCRDEGGEIRGHLNACRHRGMQVCRAEM
GNTSHFRCPYHGWTYSNTGSLVGVPAGKDAYGNQLKKSDWNLRPMPNLAS
YKGLIFGSLDPHADSLEDYLGDLKFYLDIVLDRSDAGLQVVGAPQRWVID
ANWKLGADNFVGDAYHTMMTHRSMVELGLAPPDPQFALYGEHIHTGHGHG
LGIIGPPPGMPLPEFMGLPENIVEELERRLTPEQVEIFRPTAFIHGTVFP
NLSIGNFLMGKDHLSAPTAFLTLRLWHPLGPDKMEVMSFFLVEKDAPDWF
KDESYKSYLRTFGISGGFEQDDAENWRSITRVMGGQFAKTGELNYQMGRG
VLEPDPNWTGPGEAYPLDYAEANQRNFLEYWMQLMLAESPL
3D structure
PDB2b1x Structure and Increased Thermostability of Rhodococcus sp. Naphthalene 1,2-Dioxygenase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H111 D213 H216 H221 D372
Catalytic site (residue number reindexed from 1) H111 D213 H216 H221 D372
Enzyme Commision number 1.14.12.12: naphthalene 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 H216 H221 D372 H216 H221 D372
BS02 FES A C88 H90 R91 C108 Y110 H111 W113 C88 H90 R91 C108 Y110 H111 W113
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:2b1x, PDBe:2b1x, PDBj:2b1x
PDBsum2b1x
PubMed16237006
UniProtQ9X3R9

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