MolNFT v1 · #9318 · protein

Refined 1.89 ångströms structure of the histidine-binding protein complexed with histidine and its relationship with many other active TRANSPORT(SLASH)CHEMOSENSORY receptors

1HSL: “Refined 1.89 ångströms structure of the histidine-binding protein complexed with histidine and its…”. X-ray diffraction, 2 ligands (HIS, CD), 5 pockets (best druggability 0.67). MolNFT v1 #9318 on GenesisL1: 3D structure, binding…

PDB: 1HSL
Type: protein
Length: 476 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine-binding protein
UniProt: P39182
Ligands: HIS, CD
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Histidine-binding protein	protein	238	37% helix, 21% strand	P39182

Ligands and binding sites

HIS · Histidine · ligand · 2 copies · chains A, B
CD · Cadmium ion · metal · 7 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.67	0.97	18	HIS
2	207	0.57	0.79	25	CD
3	167	0.46	0.76	22	empty
4	74	0.31	0.74	15	empty
5	53	0.29	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 451 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1HSL · Refined 1.89 ångströms structure of the histidine-binding protein complexed with… · 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 P39182
Elsewhere: RCSB PDB 1HSL · PDBe 1HSL · UniProt P39182

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