Research workbench

Human aldolase a I98S

Analyse Human aldolase a I98S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XMM
Type: protein
Length: 706 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: 7 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	353	44% helix, 15% strand	P04075
B	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	353	44% helix, 16% strand	P04075

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A, B
GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

7 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	712	0.77	0.82	91	PO4, GOL
2	441	0.73	0.83	42	PO4
3	368	0.68	0.81	42	PO4, GOL
4	146	0.57	0.83	29	empty
5	130	0.54	0.82	30	empty

Interfaces

1 interface between chains.

A–B · 847 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6XMM · Human aldolase A I98S · 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 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 P04075
Elsewhere: RCSB PDB 6XMM · PDBe 6XMM · UniProt P04075

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