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Crystal structure of scapharca inaequivalvis hbi, M37V mutant in the absence of ligand

Analyse Crystal structure of scapharca inaequivalvis hbi, M37V mutant in the absence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GRF
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
Pockets: 1 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Globin-1	protein	145	83% helix, 0% strand	P02213

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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	952	0.88	0.89	74	HEM

Interfaces

1 interface between chains.

A–B · 1032 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2GRF · Crystal structure of Scapharca inaequivalvis HBI, M37V mutant in the absence of ligand · 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 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 P02213
Elsewhere: RCSB PDB 2GRF · PDBe 2GRF · UniProt P02213

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