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Crystal structure of pmsf-treated human chymase at 1.9 ångströms resolution

Analyse Crystal structure of pmsf-treated human chymase at 1.9 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KLT
Type: protein
Length: 226 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chymase
EC: 3.4.21.39
UniProt: P23946
Ligands: PMS
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chymase (EC 3.4.21.39)	protein	226	9% helix, 38% strand	P23946

Ligands and binding sites

PMS · phenylmethanesulfonic acid · 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	108	0.44	0.78	28	PMS

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

1KLT · Crystal structure of pmsf-treated human chymase at 1.9 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P23946 · AlphaFold monomer V2.0 prediction for chymase (P23946) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23946
Elsewhere: RCSB PDB 1KLT · PDBe 1KLT · UniProt P23946

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