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3.28 a structure of the rabbit muscle aldolase

Analyse 3.28 a structure of the rabbit muscle aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VDC
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: 17 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 46% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Fructose-bisphosphate aldolase a (EC 4.1.2.13)	protein	343	46% helix, 12% strand	P00883

Pockets

17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	175	0.78	0.94	39	empty
2	168	0.77	0.93	35	empty
3	160	0.76	0.93	32	empty
4	128	0.75	0.94	31	empty
5	129	0.71	0.92	29	empty

Interfaces

6 interfaces between chains.

B–D · 1226 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 1200 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1142 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 1116 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 28 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7VDC · 3.28 A structure of the rabbit muscle aldolase · 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 A against A, TM-score 0.99

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 7VDC · PDBe 7VDC · UniProt P00883

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