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The prostaphopain B structure

Analyse The prostaphopain B structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1X9Y
Type: protein
Length: 1,384 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine proteinase
EC: 3.4.22.-
UniProt: Q70UQ8
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cysteine proteinase (EC 3.4.22.-)	protein	346	23% helix, 32% strand	Q70UQ8

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	80	0.75	0.98	25	empty
2	73	0.74	0.98	25	empty
3	76	0.74	0.97	24	empty
4	60	0.74	0.99	16	empty
5	67	0.73	0.98	19	empty

Interfaces

4 interfaces between chains.

B–C · 711 Å² buried · 9 hydrogen bonds · protein-protein
A–D · 681 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 354 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 126 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1X9Y · The prostaphopain B structure · 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 Q70UQ8
Elsewhere: RCSB PDB 1X9Y · PDBe 1X9Y · UniProt Q70UQ8

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