Structure of PDB 1ycg Chain C

Receptor sequence

>1ycgC (length=398) Species: 1525 (Moorella thermoacetica)

SQPVAITDGIYWVGAVDWNIRYFHGPAFSTHRGTTYNAYLIVDDKTALVD
TVYEPFKEELIAKLKQIKDPVKLDYLVVNHTESDHAGAFPAIMELCPDAH
VLCTQRAFDSLKAHYSHIDFNYTIVKTGTSVSLGKRSLTFIEAPMLHWPD
SMFTYVPEEALLLPNDAFGQHIATSVRFDDQVDAGLIMDEAAKYYANILM
PFSNLITKKLDEIQKINLAIKTIAPSHGIIWRKDPGRIIEAYARWAEGQG
KAKAVIAYDTMWLSTEKMAHALMDGLVAGGCEVKLFKLSVSDRNDVIKEI
LDARAVLVGSPTINNDILPVVSPLLDDLVGLRPKNKVGLAFGAYGWGGGA
QKILEERLKAAKIELIAEPGPTVQWVPRGEDLQRCYELGRKIAARIAD

3D structure

• PDB: 1ycg X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase.
• Chain: C
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H25 H81 E83 D85 H148 D167 Y195 H228
• Catalytic site (residue number reindexed from 1): H24 H80 E82 D84 H147 D166 Y194 H227
• Enzyme Commision number: 1.-.-.-

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	ZN	C	H271 D275	H270 D274
BS02	FEO	C	H81 E83 D85 H86 H148 D167 H228	H80 E82 D84 H85 H147 D166 H227
BS03	FMN	C	T261 M262 W263 S265 T266 P312 T313 I314 N315 N316 A344 Y345 G346 W347 G349 W376	T260 M261 W262 S264 T265 P311 T312 I313 N314 N315 A343 Y344 G345 W346 G348 W375
BS04	FMN	C	H25 E83 H148 W149	H24 E82 H147 W148

Gene Ontology

Molecular Function

• GO:0009055 electron transfer activity
• GO:0010181 FMN binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

External links

• PDB: RCSB:1ycg, PDBe:1ycg, PDBj:1ycg
• PDBsum: 1ycg
• PubMed: 15850383
• UniProt: Q9FDN7|FPRA_MOOTA Nitric oxide reductase (Gene Name=fprA)