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Maltoporin from salmonella typhimurium

Analyse Maltoporin from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MPR
Type: protein
Length: 1,263 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltoporin
UniProt: P26466
Ligands: CA
Pockets: 13 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 66% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Maltoporin	protein	421	1% helix, 66% strand	P26466

Ligands and binding sites

CA · Calcium ion · metal · chains A, B, C

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

Pockets

13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.79	0.99	18	empty
2	580	0.63	0.74	58	empty
3	558	0.62	0.74	60	empty
4	553	0.61	0.74	59	empty
5	132	0.44	0.76	17	empty

Interfaces

3 interfaces between chains.

A–B · 1952 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1943 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 1936 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1MPR · Maltoporin from salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
P26466 · AlphaFold monomer V2.0 prediction for maltoporin (P26466) · a predicted model of the same protein · chain A against A, 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 P26466
Elsewhere: RCSB PDB 1MPR · PDBe 1MPR · UniProt P26466

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