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Crystal structure of hscarg from homo sapiens in complex with NADP

Analyse Crystal structure of hscarg from homo sapiens in complex with NADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EXX
Type: protein
Length: 584 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hscarg protein
Ligands: NAP
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hscarg protein	protein	305	45% helix, 16% strand	—
B	Hscarg protein	protein	279	43% helix, 17% strand	—

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A, B
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1091	0.86	0.87	105	NAP, GOL
2	205	0.57	0.79	35	empty
3	119	0.56	0.83	20	empty
4	51	0.47	0.85	13	empty
5	54	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1306 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2EXX · Crystal structure of HSCARG from Homo sapiens in complex with NADP · 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 2EXX · PDBe 2EXX

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