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Structure of an inner membrane protein required for phopq regulated increases in outer membrane cardiolipin

Analyse Structure of an inner membrane protein required for phopq regulated increases… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6V8Q
Type: protein
Length: 1,134 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P40709
Ligands: QSR, CA, PO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	569	—	P40709
B	—	protein	565	—	P40709

Ligands and binding sites

QSR · (9Z,21R,24R,30R,33R,44Z)-24,27,30-trihydroxy-18,24,30, 36-tetraoxo-19,23,25,29,31,35-hexaoxa-24lambda~5~, 30lambda~5~-diphosphatripentaconta-9,44-diene-21,33-diyl (9z,9'z)di-octadec-9-enoate · ligand · 4 copies · chains A, B
CA · Calcium ion · metal · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A, B
LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains A, B

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

Compared structures

6V8Q · Structure of an inner membrane protein required for PhoPQ regulated increases in outer… · the same entry in another collection · chain A against A, TM-score 1.00
P40709 · AlphaFold monomer V2.0 prediction for inner membrane protein yejm (P40709) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P40709
Elsewhere: RCSB PDB 6V8Q · PDBe 6V8Q · UniProt P40709

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