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Structural plasticity in the eight-helix fold of a trematode hemoglobin

Analyse Structural plasticity in the eight-helix fold of a trematode hemoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KFR
Type: protein
Length: 147 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemoglobin
UniProt: P80721
Ligands: HEM, SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemoglobin	protein	147	75% helix, 0% strand	P80721

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.74	0.86	30	HEM

Compared structures

1KFR · Structural plasticity in the eight-helix fold of a trematode hemoglobin · the same entry in another collection · chain A against A, TM-score 1.00
P80721 · AlphaFold monomer V2.0 prediction for globin-3 (P80721) · 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 P80721
Elsewhere: RCSB PDB 1KFR · PDBe 1KFR · UniProt P80721

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