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HAP2 from cyanidioschyzon merolae

Analyse HAP2 from cyanidioschyzon merolae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7S0K
Type: protein
Length: 485 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HAP2-GCS1 domain-containing protein
UniProt: M1V8A6
Ligands: NAG, BMA, MAN
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HAP2-GCS1 domain-containing protein	protein	485	9% helix, 40% strand	M1V8A6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
BMA · beta-D-mannopyranose · sugar · 2 copies
MAN · alpha-D-mannopyranose · sugar
GOL · Glycerol · additive · 3 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.32	0.75	18	empty

Modifications

Observed in the structure: 9 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

7S0K · HAP2 from Cyanidioschyzon merolae · 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 M1V8A6
Elsewhere: RCSB PDB 7S0K · PDBe 7S0K · UniProt M1V8A6

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