Research workbench

NADP complex of pyrroline-5-carboxylate reductase from neisseria meningitidis

Analyse NADP complex of pyrroline-5-carboxylate reductase from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AG8
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyrroline-5-carboxylate reductase
UniProt: Q9K1N1
Ligands: NAP
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyrroline-5-carboxylate reductase	protein	263	54% helix, 14% strand	Q9K1N1

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.45	0.72	32	empty
2	144	0.42	0.75	25	NAP
3	65	0.28	0.73	14	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

2AG8 · NADP complex of Pyrroline-5-carboxylate reductase from Neisseria meningitidis · 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 Q9K1N1
Elsewhere: RCSB PDB 2AG8 · PDBe 2AG8 · UniProt Q9K1N1

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