Structure of PDB 7mgn Chain A

Receptor sequence

>7mgnA (length=522) Species: 78245 (Xanthobacter autotrophicus Py2)

KVWNARNDHLTINQWATRIDEILEAPDGGEVIYNVDENDPREYDAIFIGG
GAAGRFGSAYLRAMGGRQLIVDRWPFLGGSCPHNACVPHHLFSDCAAELM
LARTFSGQYWFPDMTEKVVGIKEVVDLFRAGRNGPHGIMNFQSKEQLNLE
YILNCPAKVIDNHTVEAAGKVFKAKNLILAVGAGPGTLDVPGVNAKGVFD
HATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRTVMLVRTEPLKL
IKDNETRAYVLDRMKEQGMEIISGSNVTRIEEDANGRVQAVVAMTPNGEM
RIETDFVFLGLGEQPRSAELAKILGLDLGPKGEVLVNEYLQTSVPNVYAV
GDLIGGPMEMFKARKSGCYAARNVMGEKISYTPKNYPDFLHTHYEVSFLG
MGEEEARAAGHEIVTIKMPPDTENGLNVALPASDRTMLYAFGKGTAHMSG
FQKIVIDAKTRKVLGAHHVGYGAKDAFQYLNVLIKQGLTVDELGDMDELH
LNPTEFIQLSRLRAGSKNLVSL

3D structure

• PDB: 7mgn The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Enzyme Commision number: 1.8.1.5: 2-oxopropyl-CoM reductase (carboxylating).

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	COM	A	A53 R56 F57 G79 C82 M140 R365	A52 R55 F56 G78 C81 M139 R364
BS02	FDA	A	G52 A54 D73 R74 W75 S81 A86 C87 H90 A158 V182 G183 H202 T225 Y229 E314 G352 D353 M359 E360 M361	G51 A53 D72 R73 W74 S80 A85 C86 H89 A157 V181 G182 H201 T224 Y228 E313 G351 D352 M358 E359 M360
BS03	MG	A	V429 L431 A447 S450	V428 L430 A446 S449

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

External links

• PDB: RCSB:7mgn, PDBe:7mgn, PDBj:7mgn
• PDBsum: 7mgn
• PubMed: 34265301
• UniProt: Q56839|XECC_XANP2 2-oxopropyl-CoM reductase, carboxylating (Gene Name=xecC)