Structure of PDB 1gjr Chain A

Receptor sequence

>1gjrA (length=295) Species: 1168 (Nostoc sp. PCC 7119) [Search protein sequence]

DVPVNLYRPNAPFIGKVISNEPLVKEGGIGIVQHIKFDLTGGNLKYIEGQ
SIGIIPPGVDKNGKPEKLRLYSIASTRHGDDVDDKTISLCVRQLEYKHPE
SGETVYGVCSTYLTHIEPGSEVKITGPVGKEMLLPDDPEANVIMLATGTG
IAPMRTYLWRMFKDAERAANPEYQFKGFSWLVFGVPTTPNILYKEELEEI
QQKYPDNFRLTYAISREQKNPQGGRMYIQDRVAEHADQLWQLIKNQKTHT
YICGLRGMEEGIDAALSAAAAKEGVTWSDYQKDLKKAGRWHVETY

3D structure

PDB

1gjr Mechanism of Coenzyme Recognition and Binding Revealed by Crystal Structure Analysis of Ferredoxin-Nadp(+) Reductase Complexed with Nadp(+)

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y79 S80 C261 E301 Y303
Catalytic site (residue number reindexed from 1)	Y71 S72 C253 E293 Y295
Enzyme Commision number	1.18.1.2: ferredoxin--NADP(+) reductase.

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	FAD	A	R77 L78 Y79 S80 C98 L102 Y104 G115 V116 C117 S118 T157 E301 Y303	R69 L70 Y71 S72 C90 L94 Y96 G107 V108 C109 S110 T149 E293 Y295
BS02	NAP	A	R100 L102 T155 G156 T157 P194 S223 R224 R233 Y235 Q237 G262 L263 Y303	R92 L94 T147 G148 T149 P186 S215 R216 R225 Y227 Q229 G254 L255 Y295

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity

View graph for
Molecular Function

External links

PDB	RCSB:1gjr, PDBe:1gjr, PDBj:1gjr
PDBsum	1gjr
PubMed	12079352
UniProt	P21890\|FENR_NOSSO Ferredoxin--NADP reductase (Gene Name=petH)

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