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Cl- binding hemoglobin component V form Propsilocerus akamusi under 500 mM NaCl at pH 4.6

Analyse Cl- binding hemoglobin component V form Propsilocerus akamusi under 500 mM NaCl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ARJ
Type: protein
Length: 152 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.81
Source: Tokunagayusurika akamusi
Molecule: Hemoglobin V
UniProt: Q7M422
Ligands: HEM, CL
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · resolution 1.81 · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemoglobin V	protein	152	76% helix, 0% strand	Q7M422

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CL · Chloride ion · ion · 5 copies · 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	186	0.70	0.87	23	HEM, CL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3ARJ · Cl- binding hemoglobin component V form propsilocerus akamusi under 500 mm nacl at pH 4.6 · 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 Q7M422
Elsewhere: RCSB PDB 3ARJ · PDBe 3ARJ · UniProt Q7M422

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