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Thermotoga maritima maltotriose binding protein, ligand free form

Analyse Thermotoga maritima maltotriose binding protein, ligand free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GHB
Type: protein
Length: 1,117 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose ABC transporter, periplasmic maltose-binding protein
Pockets: 7 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maltose ABC transporter, periplasmic maltose-binding protein	protein	373	49% helix, 21% strand	—
B, C	Maltose ABC transporter, periplasmic maltose-binding protein	protein	372	49% helix, 22% strand	—

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	895	0.74	0.78	82	empty
2	478	0.64	0.77	60	empty
3	123	0.51	0.80	27	empty
4	124	0.41	0.75	25	empty
5	75	0.35	0.76	15	empty

Interfaces

3 interfaces between chains.

A–C · 468 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 411 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 131 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2GHB · Thermotoga maritima maltotriose binding protein, ligand free form · the same entry in another collection · 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
Elsewhere: RCSB PDB 2GHB · PDBe 2GHB

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