Research workbench

Thermotoga maritima impase TM1415

Analyse Thermotoga maritima impase TM1415 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P3V
Type: protein
Length: 1,016 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inositol-1-monophosphatase
EC: 3.1.3.25
UniProt: O33832
Ligands: SRT
Pockets: 14 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Inositol-1-monophosphatase (EC 3.1.3.25)	protein	254	37% helix, 26% strand	O33832

Ligands and binding sites

SRT · S,R meso-tartaric acid · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

14 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	492	0.82	0.89	59	empty
2	370	0.80	0.89	49	empty
3	527	0.74	0.82	59	SRT
4	165	0.69	0.88	19	empty
5	350	0.68	0.82	37	SRT

Interfaces

6 interfaces between chains.

C–D · 1814 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 1747 Å² buried · 28 hydrogen bonds · protein-protein
A–D · 491 Å² buried · 1 hydrogen bond · protein-protein
B–C · 474 Å² buried · 1 hydrogen bond · protein-protein
B–D · 460 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2P3V · Thermotoga maritima IMPase TM1415 · the same entry in another collection · chain A against A, TM-score 1.00
O33832 · AlphaFold monomer V2.0 prediction for fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphata… · a predicted model of the same protein · chain B 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 O33832
Elsewhere: RCSB PDB 2P3V · PDBe 2P3V · UniProt O33832

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