MolNFT v1 · #69768 · protein

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from bartonella henselae with bound NAD

3L0D · Glyceraldehyde 3-phosphate dehydrogenase: “Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from bartonella henselae with bound NAD”. X-ray diffraction, 1 ligand (NAD), 3 pockets (best druggability 0.62). MolNFT v1…

PDB: 3L0D
Type: protein
Length: 664 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glyceraldehyde 3-phosphate dehydrogenase
EC: 1.2.1.12
UniProt: Q8L201
Ligands: NAD
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12)	protein	332	30% helix, 27% strand	Q8L201

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	424	0.62	0.77	37	NAD
2	359	0.58	0.76	39	NAD
3	52	0.28	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 1856 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

3L0D · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Bartonella henselae… · 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 Q8L201
Elsewhere: RCSB PDB 3L0D · PDBe 3L0D · UniProt Q8L201

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