Structure of PDB 2c3d Chain B

Receptor sequence
>2c3dB (length=522) Species: 78245 (Xanthobacter autotrophicus Py2) [Search protein sequence]
KVWNARNDHLTINQWATRIDEILEAPDGGEVIYNVDENDPREYDAIFIGG
GAAGRFGSAYLRAMGGRQLIVDRWPFLGGSCPHNACVPHHLFSDCAAELM
LARTFSGQYWFPDMTEKVVGIKEVVDLFRAGRNGPHGIMNFQSKEQLNLE
YILNCPAKVIDNHTVEAAGKVFKAKNLILAVGAGPGTLDVPGVNAKGVFD
HATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRTVMLVRTEPLKL
IKDNETRAYVLDRMKEQGMEIISGSNVTRIEEDANGRVQAVVAMTPNGEM
RIETDFVFLGLGEQPRSAELAKILGLDLGPKGEVLVNEYLQTSVPNVYAV
GDLIGGPMEMFKARKSGCYAARNVMGEKISYTPKNYPDFLHTHYEVSFLG
MGEEEARAAGHEIVTIKMPPDTENGLNVALPASDRTMLYAFGKGTAHMSG
FQKIVIDAKTRKVLGAHHVGYGAKDAFQYLNVLIKQGLTVDELGDMDELF
LNPTHFIQLSRLRAGSKNLVSL
3D structure
PDB2c3d Mechanistic Implications of the Structure of the Mixed-Disulfide Intermediate of the Disulfide Oxidoreductase, 2-Ketopropyl-Coenzyme M Oxidoreductase/Carboxylase.
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A53 L78 C82 C87 H90 F112 P113 H137 K224 E228 R365 F501 N503 I508
Catalytic site (residue number reindexed from 1) A52 L77 C81 C86 H89 F111 P112 H136 K223 E227 R364 F500 N502 I507
Enzyme Commision number 1.8.1.5: 2-oxopropyl-CoM reductase (carboxylating).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0016491 oxidoreductase activity
GO:0050628 2-oxopropyl-CoM reductase (carboxylating) activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0042208 propylene catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2c3d, PDBe:2c3d, PDBj:2c3d
PDBsum2c3d
PubMed16388586
UniProtQ56839|XECC_XANP2 2-oxopropyl-CoM reductase, carboxylating (Gene Name=xecC)

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