MolNFT v1 · #13564 · protein

Oxy hemoglobin (90% relative humidity)

1LFT · Hemoglobin alpha chain: “Oxy hemoglobin (90% relative humidity)”. X-ray diffraction, 1 ligand (HEM), 4 pockets (best druggability 0.75). MolNFT v1 #13564 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LFT
Type: protein
Length: 287 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemoglobin alpha chain; Hemoglobin beta chain
UniProt: P69905, P68871
Ligands: HEM
Pockets: 4 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemoglobin alpha chain	protein	141	74% helix, 0% strand	P69905
B	Hemoglobin beta chain	protein	146	80% helix, 0% strand	P68871

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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	227	0.75	0.89	29	HEM
2	219	0.69	0.85	24	HEM
3	259	0.55	0.77	34	empty
4	71	0.30	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 888 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1LFT · Oxy hemoglobin (90% relative humidity) · 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 1LFT · PDBe 1LFT · UniProt P69905 · UniProt P68871

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