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Structure of myoglobin mb-yqr 316 ns after photolysis of carbon monoxide solved from laue data at rt.

Analyse Structure of myoglobin mb-yqr 316 ns after photolysis of carbon monoxide solved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MZ0
Type: protein
Length: 154 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P02185
Ligands: HEM, SO4, CMO
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myoglobin	protein	154	79% helix, 0% strand	P02185

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · 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	246	0.73	0.87	33	HEM, CMO

Compared structures

1MZ0 · STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE… · 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 P02185
Elsewhere: RCSB PDB 1MZ0 · PDBe 1MZ0 · UniProt P02185

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