Research workbench

Rabbit muscle aldolase using 200KEV

Analyse Rabbit muscle aldolase using 200KEV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VY5
Type: protein
Length: 1,372 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase a
EC: 4.1.2.13
UniProt: P00883
Pockets: 15 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, D	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	343	48% helix, 17% strand	P00883

Pockets

15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	766	0.79	0.83	96	empty
2	783	0.79	0.82	106	empty
3	351	0.78	0.89	49	empty
4	304	0.77	0.89	46	empty
5	145	0.72	0.91	41	empty

Interfaces

6 interfaces between chains.

B–D · 1220 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 1216 Å² buried · 26 hydrogen bonds · protein-protein
C–D · 1087 Å² buried · 12 hydrogen bonds · protein-protein
B–A · 1085 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 35 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5VY5 · Rabbit muscle aldolase using 200keV · the same entry in another collection · chain D against D, TM-score 1.00
P00883 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P00883) · 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 P00883
Elsewhere: RCSB PDB 5VY5 · PDBe 5VY5 · UniProt P00883

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