MolNFT v2 · #169437 · protein

TTLL6 bound to alpha-elongation analog

6VZU: “TTLL6 bound to alpha-elongation analog”. X-ray diffraction at 1.98, 5 ligands (RZP, ADP, RZV). MolNFT v2 #169437 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6VZU
Type: protein
Length: 1,638 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.98
Source: Mus musculus
UniProt: A4Q9E8
Ligands: RZP, ADP, RZV, MG, CL

Structure

x-ray diffraction · resolution 1.98 · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	—	protein	405	—	A4Q9E8
B	—	protein	404	—	A4Q9E8
C	—	protein	396	—	A4Q9E8
M	—	protein	13	—	—
N	—	protein	15	—	—

Ligands and binding sites

RZP · (2~{S})-2-[[[(1~{R})-1-acetamido-4-oxidanyl-4-oxidanylidene-butyl]-phosphonooxy-phosphoryl]methyl]pentanedioic acid · ligand · 4 copies · chains A, C, B, D
ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
RZV · (2~{S})-2-[[[(1~{R})-1-acetamido-4-oxidanyl-4-oxidanylidene-butyl]-oxidanyl-phosphoryl]methyl]pentanedioic acid · ligand · chains C
MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
CL · Chloride ion · ion · 2 copies · chains A, D
GOL · Glycerol · additive · 16 copies · chains A, B, C, D

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

Compared structures

6VZU · TTLL6 bound to alpha-elongation analog · the same entry in another collection · chain A against A, TM-score 1.00

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 A4Q9E8
Elsewhere: RCSB PDB 6VZU · PDBe 6VZU · UniProt A4Q9E8

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