MolNFT v1 · #161632 · protein

2-naphthoyl-CoA REDUCTASE(NCR)

6QKG · Ncr a: “2-naphthoyl-CoA REDUCTASE(NCR)”. X-ray diffraction, 3 ligands (SF4, FAD, FMN), 7 pockets (best druggability 0.84). MolNFT v1 #161632 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6QKG
Type: protein
Length: 1,325 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ncr a
UniProt: E1YD54
Ligands: SF4, FAD, FMN
Pockets: 7 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ncr a	protein	661	36% helix, 19% strand	E1YD54
B	Ncr a	protein	664	35% helix, 19% strand	E1YD54

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, B
FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	421	0.84	0.91	53	FMN
2	419	0.83	0.91	56	FMN
3	479	0.81	0.88	73	FAD
4	498	0.80	0.87	72	FAD
5	234	0.60	0.80	29	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6QKG · 2-Naphthoyl-CoA Reductase(NCR) · the same entry in another collection · chain A against A, 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 E1YD54
Elsewhere: RCSB PDB 6QKG · PDBe 6QKG · UniProt E1YD54

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