MolNFT v1 · #153554 · protein

Crystal structure of archaeal ribosomal protein AP1, apelota, and GTP- bound AEF1A complex

6JI2: “Crystal structure of archaeal ribosomal protein AP1, apelota, and GTP- bound AEF1A complex”. X-ray diffraction, 3 ligands (GTP, MG, NA). MolNFT v1 #153554 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6JI2
Type: protein
Length: 1,587 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9YAV0, Q9YAZ5
Ligands: GTP, MG, NA

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	—	protein	432	—	Q9YAV0
B, F	—	protein	357	—	Q9YAZ5
X	—	protein	9	—	—

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, E
MG · Magnesium ion · metal · 2 copies · chains A, E
NA · Sodium ion · metal · 2 copies · chains A, E

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

Compared structures

6JI2 · Crystal structure of archaeal ribosomal protein aP1, aPelota, and GTP-bound aEF1A complex · the same entry in another collection · chain X against X, TM-score 1.00
Q9YAV0 · AlphaFold monomer V2.0 prediction for elongation factor 1-alpha (Q9YAV0) · a predicted model of the same protein · chain E against A, TM-score 0.99
Q9YAZ5 · AlphaFold monomer V2.0 prediction for protein pelota homolog (Q9YAZ5) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q9YAV0
Every structure of UniProt Q9YAZ5
Elsewhere: RCSB PDB 6JI2 · PDBe 6JI2 · UniProt Q9YAV0 · UniProt Q9YAZ5

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