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The monomeric structure of G80A/H81A/H82A myoglobin

Analyse The monomeric structure of G80A/H81A/H82A myoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LS8
Type: protein
Length: 918 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P68082
Ligands: HEM
Pockets: 13 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K	Myoglobin	protein	153	76% helix, 0% strand	P68082

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 6 copies · chains A, C, E, G, I, K

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	838	0.82	0.85	82	HEM
2	214	0.73	0.88	36	HEM
3	188	0.72	0.88	27	HEM
4	199	0.71	0.87	30	HEM
5	520	0.69	0.79	50	HEM

Interfaces

9 interfaces between chains.

C–K · 487 Å² buried · 3 hydrogen bonds · protein-protein
E–K · 395 Å² buried · 2 hydrogen bonds · protein-protein
E–G · 330 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 320 Å² buried · 9 hydrogen bonds · protein-protein
A–I · 298 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6LS8 · The monomeric structure of G80A/H81A/H82A myoglobin · the same entry in another collection · chain A against A, TM-score 1.00

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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 6LS8 · PDBe 6LS8 · UniProt P68082

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