MolNFT v1 · #169767 · protein

Human aldolase a wild type

6XMH · Fructose-bisphosphate aldolase a: “Human aldolase a wild type”. X-ray diffraction, 1 ligand (PO4), 8 pockets (best druggability 0.76). MolNFT v1 #169767 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XMH
Type: protein
Length: 707 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase a
EC: 4.1.2.13
UniProt: P04075
Ligands: PO4
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	356	46% helix, 15% strand	P04075
B	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	351	45% helix, 16% strand	P04075

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A, B
GOL · Glycerol · additive · 7 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	617	0.76	0.82	68	GOL
2	412	0.70	0.82	55	PO4
3	170	0.62	0.84	35	PO4
4	162	0.59	0.83	26	empty
5	150	0.54	0.81	29	GOL

Interfaces

1 interface between chains.

A–B · 837 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6XMH · Human aldolase A wild type · the same entry in another collection · chain A against A, TM-score 1.00
P04075 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P04075) · a predicted model of the same protein · chain B 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 P04075
Elsewhere: RCSB PDB 6XMH · PDBe 6XMH · UniProt P04075

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