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Crystal structure of hpr-C-his from thermoanaerobacter tengcongensis

Analyse Crystal structure of hpr-C-his from thermoanaerobacter tengcongensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LFG
Type: protein
Length: 265 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotransferase system, hpr-related proteins
UniProt: Q8R910
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Phosphotransferase system, hpr-related proteins	protein	88	39% helix, 26% strand	Q8R910
B	Phosphotransferase system, hpr-related proteins	protein	89	38% helix, 26% strand	Q8R910

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	346	0.58	0.76	39	empty

Interfaces

2 interfaces between chains.

A–B · 426 Å² buried · 1 hydrogen bond · protein-protein
B–C · 253 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3LFG · Crystal structure of HPr-C-His from Thermoanaerobacter tengcongensis · 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
Every structure of UniProt Q8R910
Elsewhere: RCSB PDB 3LFG · PDBe 3LFG · UniProt Q8R910

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