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Manganese horse heart myoglobin, methanol modified

Analyse Manganese horse heart myoglobin, methanol modified in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O5L
Type: protein
Length: 152 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P68082
Ligands: MNR, SO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Myoglobin	protein	152	75% helix, 0% strand	P68082

Ligands and binding sites

MNR · Protoporphyrin IX containing Mn · ligand · chains X
SO4 · Sulfate ion · ion · 2 copies · chains X
MOH · Methanol · additive · chains X

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	221	0.71	0.86	28	MNR, MOH

Compared structures

2O5L · Manganese horse heart myoglobin, methanol modified · the same entry in another collection · chain X against X, 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 P68082
Elsewhere: RCSB PDB 2O5L · PDBe 2O5L · UniProt P68082

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