MolNFT v1 · #5107 · protein

Crystal structure of the EMAP2/RNA binding domain of the P43 protein from human aminoacyl-tRNA synthetase complex

1E7Z · Endothelial-monocyte activating polypeptide II: “Crystal structure of the EMAP2/RNA binding domain of the P43 protein from human aminoacyl-tRNA synthetase…”. X-ray diffraction, 1 ligand (HG), 2 pockets (best druggability 0.46).…

PDB: 1E7Z
Type: protein
Length: 173 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endothelial-monocyte activating polypeptide II
UniProt: Q12904
Ligands: HG
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endothelial-monocyte activating polypeptide II	protein	173	12% helix, 36% strand	Q12904

Ligands and binding sites

HG · Mercury (II) ion · metal · 2 copies · chains A

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	153	0.46	0.76	23	empty
2	59	0.38	0.80	14	empty

Compared structures

1E7Z · Crystal structure of the EMAP2/RNA binding domain of the p43 protein from human… · the same entry in another collection · chain A against A, TM-score 1.00
Q12904 · AlphaFold monomer V2.0 prediction for aminoacyl tRNA synthase complex-interacting… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q12904
Elsewhere: RCSB PDB 1E7Z · PDBe 1E7Z · UniProt Q12904

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