Research workbench

Human oxy-hemoglobin

Analyse Human oxy-hemoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BB5
Type: protein
Length: 284 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemoglobin subunit alpha; Hemoglobin subunit beta
UniProt: P69905, P68871
Ligands: HEM, OXY
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemoglobin subunit alpha	protein	139	78% helix, 0% strand	P69905
B	Hemoglobin subunit beta	protein	145	77% helix, 0% strand	P68871

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
OXY · Oxygen molecule · ion · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	210	0.73	0.88	26	HEM, OXY
2	173	0.68	0.86	24	HEM, OXY
3	115	0.51	0.81	22	empty
4	57	0.36	0.79	13	empty

Interfaces

1 interface between chains.

A–B · 921 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6BB5 · Human Oxy-Hemoglobin · 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 P69905
Every structure of UniProt P68871
Elsewhere: RCSB PDB 6BB5 · PDBe 6BB5 · UniProt P69905 · UniProt P68871

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.