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Carbonmonoxy human hemoglobin C in the R quaternary structure at 95 K: light (2 min)

Analyse Carbonmonoxy human hemoglobin C in the R quaternary structure at 95 K: light (2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L5V
Type
protein
Length
287 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P69905, P68871
Ligands
HEM, CMO

Structure

x-ray diffraction · 2 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein141—P69905
B—protein146—P68871

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
  • CMO · Carbon monoxide · ion · 2 copies · chains A, B

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

Compared structures

  • 6L5V · Carbonmonoxy human hemoglobin C in the R quaternary structure at 95 K: Light (2 min) · the same entry in another collection · chain A against A, TM-score 1.00

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