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Homo sapiens prolyl-tRNA synthetase (hsprs) in complex with L-proline and compound L96

Analyse Homo sapiens prolyl-tRNA synthetase (hsprs) in complex with L-proline and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F9C
Type: protein
Length: 976 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P07814
Ligands: 1UI, CA, ZN, CL

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	489	—	P07814
B	—	protein	487	—	P07814

Ligands and binding sites

1UI · 4-[(3S)-3-cyano-3-cyclopropyl-2-oxidanylidene-pyrrolidin-1-yl]-N-[[3-fluoranyl-5-(5-methoxypyridin-3-yl)phenyl]methyl]-6-methyl-pyridine-2-carboxamide · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 6 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 4 copies · chains A, B

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

Compared structures

7F9C · Homo sapiens Prolyl-tRNA Synthetase (HsPRS) in Complex with L-proline and compound L96 · the same entry in another collection · chain A against A, TM-score 1.00
P07814 · AlphaFold monomer V2.0 prediction for bifunctional GLUTAMATE/PROLINE --tRNA ligase… · a predicted model of the same protein · chain A 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 P07814
Elsewhere: RCSB PDB 7F9C · PDBe 7F9C · UniProt P07814

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