MolNFT v1 · #54499 · protein

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

2XQU · ATP synthase C chain: “Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases”. X-ray diffraction, 1 ligand (CVM). MolNFT v1 #54499 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2XQU
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

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 · 55 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.

B–C · 1931 Å² buried · 16 hydrogen bonds · protein-protein
D–E · 1921 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 1907 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 1880 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (formylation).

Compared structures

2XQU · 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 2XQU · PDBe 2XQU · UniProt D5A0Q7

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