MolNFT v1 · #18874 · protein

Crystal structure of pitrilysin

1Q2L · Protease III: “Crystal structure of pitrilysin”. X-ray diffraction, 2 ligands (PT, ZN), 12 pockets (best druggability 0.66). MolNFT v1 #18874 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1Q2L
Type: protein
Length: 937 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease III
EC: 3.4.24.55
UniProt: P05458
Ligands: PT, ZN
Pockets: 12 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease III (EC 3.4.24.55)	protein	937	44% helix, 20% strand	P05458

Ligands and binding sites

PT · Platinum (II) ion · metal · 6 copies · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	442	0.66	0.79	48	empty
2	653	0.66	0.75	53	empty
3	253	0.58	0.79	42	empty
4	141	0.57	0.83	23	empty
5	236	0.56	0.78	25	empty

Compared structures

1Q2L · Crystal Structure of pitrilysin · the same entry in another collection · chain A against A, TM-score 1.00
P05458 · AlphaFold monomer V2.0 prediction for protease 3 (P05458) · a predicted model of the same protein · chain A against A, TM-score 0.64

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 P05458
Elsewhere: RCSB PDB 1Q2L · PDBe 1Q2L · UniProt P05458

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