MolNFT v1 · #122443 · protein

Human histidine triad nucleotide binding protein 1 (HHINT1) H112N mutant

5IPB · Histidine triad nucleotide-binding protein 1: “Human histidine triad nucleotide binding protein 1 (HHINT1) H112N mutant”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.33). MolNFT v1 #122443 on GenesisL1: 3D…

PDB: 5IPB
Type: protein
Length: 228 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine triad nucleotide-binding protein 1
EC: 3.-.-.-
UniProt: P49773
Ligands: CL
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-)	protein	115	29% helix, 24% strand	P49773
B	Histidine triad nucleotide-binding protein 1 (EC 3.-.-.-)	protein	113	29% helix, 25% strand	P49773

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.33	0.75	22	empty
2	73	0.31	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 1991 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

5IPB · Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) H112N mutant · 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 P49773
Elsewhere: RCSB PDB 5IPB · PDBe 5IPB · UniProt P49773

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