MolNFT v1 · #91242 · protein

Crystal structure of ferredoxin-NADP reductase from burkholderia thailandensis E264

4F7D · Ferredoxin--NADP reductase: “Crystal structure of ferredoxin-NADP reductase from burkholderia thailandensis E264”. X-ray diffraction, 6 pockets (best druggability 0.66). MolNFT v1 #91242 on GenesisL1: 3D structure, binding sites and…

PDB: 4F7D
Type: protein
Length: 493 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin--NADP reductase
EC: 1.18.1.2
UniProt: Q2T230
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	246	27% helix, 32% strand	Q2T230
B	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	247	28% helix, 33% strand	Q2T230

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	364	0.66	0.80	57	empty
2	155	0.58	0.82	20	empty
3	76	0.57	0.87	28	empty
4	60	0.39	0.79	15	empty
5	90	0.33	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 861 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4F7D · Crystal structure of ferredoxin-NADP reductase from burkholderia thailandensis E264 · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q2T230
Elsewhere: RCSB PDB 4F7D · PDBe 4F7D · UniProt Q2T230

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