PDBsum entry 7f9c

Ligase/ligase inhibitor

PDB id: 7f9c

Contents

Protein chains

488 a.a.

Ligands

1UI ×2

PRO ×2

_CA ×6

Metals

_ZN ×2

_CL ×4

Waters ×174

PDB id:

7f9c

Name:

Ligase/ligase inhibitor

Title:

Homo sapiens prolyl-tRNA synthetase (hsprs) in complex with l-proline and compound l96

Structure:

Bifunctional glutamate/proline--tRNA ligase. Chain: a, b. Synonym: bifunctional aminoacyl-tRNA synthetase,cell proliferation- inducing gene 32 protein,glutamatyl-prolyl-tRNA synthetase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: eprs1, eprs, glns, pars, qars, qprs, pig32. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.20Å R-factor: 0.191 R-free: 0.253

Authors:

N.Malhotra,Y.Manickam,A.Sharma

Key ref:

N.Malhotra et al. Hsprs with ATP binding pocket inhibitor. To be published, . PubMed id: 36854028

Date:

04-Jul-21 Release date: 06-Jul-22

Protein chains

P07814  (SYEP_HUMAN) -  Bifunctional glutamate/proline--tRNA ligase from Homo sapiens

Seq: 1512 a.a.

Struc: 488 a.a.

Enzyme reactions

• Enzyme class 1: E.C.6.1.1.15 - proline--tRNA ligase.
• Reaction: tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + diphosphate

tRNA(Pro) + L-proline (Bound ligand (Het Group name = PRO) corresponds exactly) + ATP = L-prolyl-tRNA(Pro) + AMP + diphosphate

• Enzyme class 2: E.C.6.1.1.17 - glutamate--tRNA ligase.
• Reaction: tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate

tRNA(Glu) + L-glutamate (Bound ligand (Het Group name = PRO) matches with 80.00% similarity) + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site