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X-ray structural investigation of leghemoglobin. VI. structure of acetate-ferrileghemoglobin at a resolution of 2.0 ångströms (russian)

Analyse X-ray structural investigation of leghemoglobin. VI. structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LH7
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leghemoglobin (nitrosobenzene)
UniProt: P02240
Ligands: HEM, NBE
Pockets: 1 · best druggability 0.76

Structure

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

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

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
NBE · Nitrosobenzene · 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	379	0.76	0.86	30	HEM, NBE

Compared structures

1LH7 · X-ray structural investigation of leghemoglobin. VI. structure of… · 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 0.96

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 1LH7 · PDBe 1LH7 · UniProt P02240

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