MolNFT v1 · #27290 · protein

Human brain fructose 1,6-(BIS)PHOSPHATE aldolase (C isozyme)

1XFB · Aldolase C: “Human brain fructose 1,6-(BIS)PHOSPHATE aldolase (C isozyme)”. X-ray diffraction, 20 pockets (best druggability 0.89). MolNFT v1 #27290 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1XFB
Type: protein
Length: 4,104 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldolase C
EC: 4.1.2.13
UniProt: P09972
Pockets: 20 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Aldolase C (EC 4.1.2.13)	protein	342	45% helix, 16% strand	P09972

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1018	0.89	0.90	116	empty
2	955	0.88	0.90	119	empty
3	896	0.88	0.90	104	empty
4	983	0.84	0.86	93	empty
5	729	0.81	0.85	77	empty

Interfaces

25 interfaces between chains.

C–D · 1358 Å² buried · 22 hydrogen bonds · protein-protein
K–L · 1351 Å² buried · 30 hydrogen bonds · protein-protein
E–F · 1348 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 1332 Å² buried · 21 hydrogen bonds · protein-protein
G–H · 1315 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

1XFB · Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme) · the same entry in another collection · chain L against L, 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 P09972
Elsewhere: RCSB PDB 1XFB · PDBe 1XFB · UniProt P09972

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