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X-ray structure of a novel thermostable hemoglobin from the actinobacterium thermobifida fusca

Analyse X-ray structure of a novel thermostable hemoglobin from the actinobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BMM
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermostable hemoglobin from thermobifida fusca
Ligands: HEM
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thermostable hemoglobin from thermobifida fusca	protein	123	68% helix, 0% strand	—

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
ACT · Acetate ion · additive · 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	363	0.79	0.88	30	HEM, ACT

Compared structures

2BMM · X-ray structure of a novel thermostable hemoglobin from the actinobacterium Thermobifida… · 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
Elsewhere: RCSB PDB 2BMM · PDBe 2BMM

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