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Crystal structure of ferric complexes of the yellow lupin leghemoglobin with isoquinoline at 1.8 ångströms resolution (russian)

Analyse Crystal structure of ferric complexes of the yellow lupin leghemoglobin with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GDI
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leghemoglobin (carbonmonoxy)
UniProt: P02240
Ligands: HEM, CMO
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leghemoglobin (carbonmonoxy)	protein	153	78% helix, 0% strand	P02240

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CMO · Carbon monoxide · ion · 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	291	0.72	0.85	32	HEM, CMO

Compared structures

1GDI · Crystal structure of ferric complexes of the yellow lupin leghemoglobin with isoquinoline… · the same entry in another collection · chain A against A, TM-score 1.00
P02240 · AlphaFold monomer V2.0 prediction for leghemoglobin-2 (P02240) · 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 P02240
Elsewhere: RCSB PDB 1GDI · PDBe 1GDI · UniProt P02240

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