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Mutant glyceraldehyde dehydrogenase (F34M+S405N) from thermoplasma acidophilum

Analyse Mutant glyceraldehyde dehydrogenase (F34M+S405N) from thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J77
Type: protein
Length: 1,968 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-glyceraldehyde dehydrogenase (NADP(+))
EC: 1.2.1.89
UniProt: Q9HK01
Pockets: 18 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	D-glyceraldehyde dehydrogenase (NADP(+)) (EC 1.2.1.89)	protein	492	42% helix, 22% strand	Q9HK01

Pockets

18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	624	0.81	0.86	68	empty
2	611	0.81	0.86	66	empty
3	325	0.69	0.83	45	empty
4	282	0.68	0.84	40	empty
5	313	0.68	0.83	42	empty

Interfaces

3 interfaces between chains.

A–B · 4237 Å² buried · 67 hydrogen bonds · protein-protein
C–D · 4202 Å² buried · 65 hydrogen bonds · protein-protein
B–C · 11 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

Q9HK01 · AlphaFold monomer V2.0 prediction for D-glyceraldehyde dehydrogenase (NADP(+)) (Q9HK01) · a predicted model of the same protein · chain D 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 Q9HK01
Elsewhere: RCSB PDB 5J77 · PDBe 5J77 · UniProt Q9HK01

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