MolNFT v1 · #54498 · protein

Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases

2XQT · ATP synthase C chain: “Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases”. X-ray diffraction, 2 ligands (CVM, DCW). MolNFT v1 #54498 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2XQT
Type: protein
Length: 410 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP synthase C chain
UniProt: D5A0Q7
Ligands: CVM, DCW

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	ATP synthase C chain	protein	82	85% helix, 0% strand	D5A0Q7

Ligands and binding sites

CVM · Cymal-4 · ligand · 45 copies · chains A, B, C, D, E
DCW · Dicyclohexylurea · ligand · 5 copies · chains A, B, C, D, E

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

Interfaces

4 interfaces between chains.

C–D · 1933 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1930 Å² buried · 14 hydrogen bonds · protein-protein
D–E · 1929 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1914 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (formylation).

Compared structures

2XQT · Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases · 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 D5A0Q7
Elsewhere: RCSB PDB 2XQT · PDBe 2XQT · UniProt D5A0Q7

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