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Crystal structure of human hisrs

Analyse Crystal structure of human hisrs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G85
Type: protein
Length: 853 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine-tRNA ligase, cytoplasmic
EC: 6.1.1.21
UniProt: P12081
Pockets: 9 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidine-tRNA ligase, cytoplasmic (EC 6.1.1.21)	protein	427	45% helix, 20% strand	P12081
B	Histidine-tRNA ligase, cytoplasmic (EC 6.1.1.21)	protein	426	42% helix, 21% strand	P12081

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	775	0.80	0.83	60	empty
2	298	0.56	0.77	38	empty
3	295	0.55	0.76	36	empty
4	149	0.51	0.79	23	empty
5	140	0.45	0.77	26	empty

Interfaces

1 interface between chains.

A–B · 3911 Å² buried · 54 hydrogen bonds · protein-protein

Compared structures

4G85 · Crystal structure of human HisRS · the same entry in another collection · chain A against A, TM-score 1.00
P12081 · AlphaFold monomer V2.0 prediction for histidine--tRNA ligase, cytoplasmic (P12081) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P12081
Elsewhere: RCSB PDB 4G85 · PDBe 4G85 · UniProt P12081

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