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Structure of the sulfide-reactive hemoglobin from the clam lucina pectinata: crystallographic analysis at 1.5 ångströms resolution

Analyse Structure of the sulfide-reactive hemoglobin from the clam lucina pectinata… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FLP
Type: protein
Length: 142 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemoglobin I (aquo met)
UniProt: P41260
Ligands: HEM
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemoglobin I (aquo met)	protein	142	77% helix, 0% strand	P41260

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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	217	0.68	0.85	26	HEM

Compared structures

1FLP · Structure of the sulfide-reactive hemoglobin from the clam lucina pectinata… · the same entry in another collection · chain A against A, TM-score 1.00
P41260 · AlphaFold monomer V2.0 prediction for hemoglobin-1 (P41260) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P41260
Elsewhere: RCSB PDB 1FLP · PDBe 1FLP · UniProt P41260

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