MolNFT v1 · #21939 · protein

Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase

1SQ7: “Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase”. X-ray diffraction, 5 pockets (best druggability 0.70). MolNFT v1 #21939 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1SQ7
Type: protein
Length: 494 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: P00940
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Triosephosphate isomerase (EC 5.3.1.1)	protein	247	44% helix, 17% strand	P00940

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.70	0.98	23	empty
2	99	0.39	0.77	22	empty
3	55	0.38	0.80	17	empty
4	54	0.32	0.77	17	empty
5	62	0.29	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1711 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

1SQ7 · Understanding protein lids: Structural analysis of active hinge mutants in… · the same entry in another collection · chain A against A, TM-score 1.00
P00940 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P00940) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P00940
Elsewhere: RCSB PDB 1SQ7 · PDBe 1SQ7 · UniProt P00940

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