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Crystal structure of apohpr monomer from thermoanaerobacter tengcongensis

Analyse Crystal structure of apohpr monomer 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: 3LE1
Type: protein
Length: 172 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotransferase system, hpr-related proteins
UniProt: Q8R910
Ligands: CD
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotransferase system, hpr-related proteins	protein	87	36% helix, 26% strand	Q8R910
B	Phosphotransferase system, hpr-related proteins	protein	85	32% helix, 27% strand	Q8R910

Ligands and binding sites

CD · Cadmium ion · metal · 6 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.31	0.73	16	CD

Interfaces

1 interface between chains.

A–B · 107 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3LE1 · Crystal structure of apoHPr monomer 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 3LE1 · PDBe 3LE1 · UniProt Q8R910

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