Structure of PDB 2c9x Chain A

Receptor sequence
>2c9xA (length=373) Species: 921 (Ancylobacter novellus) [Search protein sequence]
ADTVTLPFANGERPLVMYPGKRPLIGLTARPPQLETPFSVFDEGLITPND
AFFVRYHLAGIPLEIDPDAFRLEIKGKVGTPLSLSLQDLKNDFPASEVVA
VNQCSGNSRGFVEPRVGGGQLANGAMGNARWRGVPLKAVLEKAGVQAGAK
QVTFGGLDGPVIPETPDFVKALSIDHATDGEVMLAYSMNGADLPWLNGYP
LRLVVPGYYGTYWVKHLNEITVIDKEFDGFWMKTAFRIPDNACACTEPGK
APTATIPINRFDVRSFITNVENGASVKAGEVPLRGIAFDGGYGITQVSVS
ADAGKSWTNATLDPGLGKYSFRGWKAVLPLTKGDHVLMCRATNARGETQP
MQATWNPAGYMRNVVEATRVIAA
3D structure
PDB2c9x Kinetic and Structural Evidence for the Importance of Tyr236 for the Integrity of the Mo Active Site in a Bacterial Sulfite Dehydrogenase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R55 C104 A235 F236
Catalytic site (residue number reindexed from 1) R55 C104 A235 F236
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 MSS A F53 V54 R55 Y56 H57 N102 C104 S105 D158 F168 N197 R202 G210 T211 W213 V214 K215 F236 F53 V54 R55 Y56 H57 N102 C104 S105 D158 F168 N197 R202 G210 T211 W213 V214 K215 F236
BS02 HEC A R55 H57 R55 H57
Gene Ontology
Molecular Function
GO:0008482 sulfite oxidase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0030151 molybdenum ion binding
GO:0043546 molybdopterin cofactor binding
GO:0046872 metal ion binding
Biological Process
GO:0006790 sulfur compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2c9x, PDBe:2c9x, PDBj:2c9x
PDBsum2c9x
PubMed16893171
UniProtQ9LA16

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