Research workbench

M37V mutant of scapharca dimeric hemoglobin, with co bound

Analyse M37V mutant of scapharca dimeric hemoglobin, with co bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GRH
Type: protein
Length: 290 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Globin-1
UniProt: P02213
Ligands: HEM, CMO
Pockets: 1 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Globin-1	protein	145	81% helix, 0% strand	P02213

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
CMO · Carbon monoxide · ion · 2 copies · chains A, B

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	894	0.86	0.88	71	HEM, CMO

Interfaces

1 interface between chains.

A–B · 961 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2GRH · M37V mutant of Scapharca dimeric hemoglobin, with CO bound · the same entry in another collection · chain A against A, TM-score 1.00
P02213 · AlphaFold monomer V2.0 prediction for globin-1 (P02213) · a predicted model of the same protein · 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 P02213
Elsewhere: RCSB PDB 2GRH · PDBe 2GRH · UniProt P02213

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