MolNFT v1 · #162278 · protein

Crystal structure of lpor (thermosynechococcus elongatus) complexed with NADP+ at 2.5A resolution

6R46 · NADPH-protochlorophyllide oxidoreductase: “Crystal structure of lpor (thermosynechococcus elongatus) complexed with NADP+ at 2.5A resolution”. X-ray diffraction, 3 ligands (NAP, ZN, CL), 1 pocket (best druggability 0.68). MolNFT v1…

PDB: 6R46
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADPH-protochlorophyllide oxidoreductase
EC: 1.3.1.33
UniProt: Q8DLC1
Ligands: NAP, ZN, CL
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADPH-protochlorophyllide oxidoreductase (EC 1.3.1.33)	protein	275	45% helix, 17% strand	Q8DLC1

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
ZN · Zinc ion · metal · 5 copies · chains A
CL · Chloride ion · ion · 4 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	520	0.68	0.78	52	NAP

Compared structures

6R46 · Crystal structure of LPOR (Thermosynechococcus elongatus) complexed with NADP+ at 2.5A… · 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 Q8DLC1
Elsewhere: RCSB PDB 6R46 · PDBe 6R46 · UniProt Q8DLC1

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