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Crystal structure of fructose-bisphosphate aldolase, class I from porphyromonas gingivalis

Analyse Crystal structure of fructose-bisphosphate aldolase, class I from porphyromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IQT
Type: protein
Length: 295 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase class 1
EC: 4.1.2.13
UniProt: P60053
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase class 1 (EC 4.1.2.13)	protein	295	48% helix, 20% strand	P60053

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	232	0.58	0.80	27	empty

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

2IQT · Crystal Structure of Fructose-Bisphosphate Aldolase, Class I from Porphyromonas gingivalis · the same entry in another collection · chain A against A, TM-score 1.00
P60053 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase class 1 (P60053) · 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 P60053
Elsewhere: RCSB PDB 2IQT · PDBe 2IQT · UniProt P60053

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