MolNFT v2 · #163180 · protein

Structure of ATP-bound outward-facing TM287/288 in complex with sybody Sb_TM35

6QV0: “Structure of ATP-bound outward-facing TM287/288 in complex with sybody Sb_TM35”. X-ray diffraction at 3.12, 2 ligands (ATP, MG). MolNFT v2 #163180 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6QV0
Type: protein
Length: 2,529 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.12
Source: synthetic construct; Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 /…
UniProt: Q9WYC3, Q9WYC4
Ligands: ATP, MG

Structure

x-ray diffraction · resolution 3.12 · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	568	—	Q9WYC3
B	—	protein	570	—	Q9WYC4
C	—	protein	569	—	Q9WYC3
D	—	protein	574	—	Q9WYC4
E, F	—	protein	124	—	—

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D

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

Compared structures

6QV0 · Structure of ATP-bound outward-facing TM287/288 in complex with sybody SB_TM35 · the same entry in another collection · chain F against F, TM-score 1.00
Q9WYC4 · AlphaFold monomer V2.0 prediction for uncharacterized ABC transporter ATP-binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.72

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 Q9WYC3
Every structure of UniProt Q9WYC4
Elsewhere: RCSB PDB 6QV0 · PDBe 6QV0 · UniProt Q9WYC3 · UniProt Q9WYC4

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