MolNFT v1 · #14881 · protein

Interactions among residues CD3, E7, E10 and E11 in myoglobins: attempts to simulate the O2 and co binding properties of aplysia myoglobin

1MNH: “Interactions among residues CD3, E7, E10 and E11 in myoglobins: attempts to simulate the O2 and co binding…”. X-ray diffraction, 1 ligand (HEM), 1 pocket (best druggability 0.70). MolNFT v1 #14881 on GenesisL1: 3D structure, binding…

PDB: 1MNH
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P02189
Ligands: HEM
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myoglobin	protein	153	80% helix, 0% strand	P02189

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · 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	236	0.70	0.85	28	HEM

Compared structures

1MNH · Interactions among residues CD3, E7, E10 and E11 in myoglobins: attempts to simulate the… · the same entry in another collection · chain A against A, TM-score 1.00
P02189 · AlphaFold monomer V2.0 prediction for myoglobin (P02189) · 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 P02189
Elsewhere: RCSB PDB 1MNH · PDBe 1MNH · UniProt P02189

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