MolNFT v1 · #112096 · protein

Crystal structure of proteinase K from engyodontium albuminhibited by methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone at 1.15 a resolution

4ZAR: “Crystal structure of proteinase K from engyodontium albuminhibited by…”. X-ray diffraction, 2 ligands (MSU, CA). MolNFT v1 #112096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4ZAR
Type: protein
Length: 283 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteinase K; Methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone, bound form
EC: 3.4.21.64
UniProt: P06873
Ligands: MSU, CA

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proteinase K (EC 3.4.21.64)	protein	279	27% helix, 25% strand	P06873
B	Methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone, bound form	protein	4	0% helix, 50% strand	—

Ligands and binding sites

MSU · Succinic acid monomethyl ester · ligand · chains A, B
CA · Calcium ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 386 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 1 covalent, 1 modified (disulfide, covalent ligand, nonstandard).

Compared structures

4ZAR · Crystal Structure of Proteinase K from Engyodontium albuminhibited by… · 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 P06873
Elsewhere: RCSB PDB 4ZAR · PDBe 4ZAR · UniProt P06873

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