BioLiP

Structure of PDB 1ycf Chain A

Receptor sequence

>1ycfA (length=398) Species: 1525 (Moorella thermoacetica) [Search protein sequence]

SQPVAITDGIYWVGAVDWNIRYFHGPAFSTHRGTTYNAYLIVDDKTALVD
TVYEPFKEELIAKLKQIKDPVKLDYLVVNHTESDHAGAFPAIMELCPDAH
VLCTQRAFDSLKAHYSHIDFNYTIVKTGTSVSLGKRSLTFIEAPMLHWPD
SMFTYVPEEALLLPNDAFGQHIATSVRFDDQVDAGLIMDEAAKYYANILM
PFSNLITKKLDEIQKINLAIKTIAPSHGIIWRKDPGRIIEAYARWAEGQG
KAKAVIAYDTMWLSTEKMAHALMDGLVAGGCEVKLFKLSVSDRNDVIKEI
LDARAVLVGSPTINNDILPVVSPLLDDLVGLRPKNKVGLAFGAYGWGGGA
QKILEERLKAAKIELIAEPGPTVQWVPRGEDLQRCYELGRKIAARIAD

3D structure

PDB

1ycf X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase.

Chain

Resolution

3.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	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)
BS01	ZN	A	H271 D275	H270 D274
BS02	FEO	A	H81 E83 D85 H86 H148 D167 H228	H80 E82 D84 H85 H147 D166 H227
BS03	OXY	A	F24 H25 Y195	F23 H24 Y194
BS04	FMN	A	T261 M262 W263 S265 T266 P312 T313 I314 N315 N316 Y345 G346 W347 G348 W376	T260 M261 W262 S264 T265 P311 T312 I313 N314 N315 Y344 G345 W346 G347 W375
BS05	FMN	A	H25 E83 W149	H24 E82 W148

Gene Ontology

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

View graph for
Molecular Function

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