MolNFT v1 · #152706 · protein

Crystal structure of prc with S452I and L252Y mutations

6IQR · Tail-specific protease: “Crystal structure of prc with S452I and L252Y mutations”. X-ray diffraction, 13 pockets (best druggability 0.85). MolNFT v1 #152706 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6IQR
Type: protein
Length: 1,275 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tail-specific protease
EC: 3.4.21.102
UniProt: P23865
Pockets: 13 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tail-specific protease (EC 3.4.21.102)	protein	639	41% helix, 16% strand	P23865
B	Tail-specific protease (EC 3.4.21.102)	protein	636	40% helix, 17% strand	P23865

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	723	0.85	0.89	79	empty
2	1071	0.85	0.86	109	empty
3	1074	0.79	0.81	97	empty
4	397	0.68	0.81	27	empty
5	327	0.65	0.81	34	empty

Interfaces

1 interface between chains.

A–B · 674 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6IQR · Crystal structure of Prc with S452I and L252Y mutations · the same entry in another collection · chain A against A, TM-score 1.00
P23865 · AlphaFold monomer V2.0 prediction for tail-specific protease (P23865) · a predicted model of the same protein · chain B against A, TM-score 0.81

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 P23865
Elsewhere: RCSB PDB 6IQR · PDBe 6IQR · UniProt P23865

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