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Pandda analysis group deposition -- proteinase K changed state model for fragment frag xtal screen H3A

Analyse Pandda analysis group deposition -- proteinase K changed state model for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5RPC
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteinase K
EC: 3.4.21.64
UniProt: P06873
Ligands: W9J
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proteinase K (EC 3.4.21.64)	protein	278	27% helix, 24% strand	P06873

Ligands and binding sites

W9J · N-carbamoyl-L-methionine · ligand · 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	92	0.37	0.76	26	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5RPC · PanDDA analysis group deposition -- Proteinase K changed state model for fragment Frag… · the same entry in another collection · chain A against A, TM-score 1.00
P06873 · AlphaFold monomer V2.0 prediction for proteinase K (P06873) · a predicted model of the same protein · 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 P06873
Elsewhere: RCSB PDB 5RPC · PDBe 5RPC · UniProt P06873

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