_EC 3.4.24.21 Astacin. 9 PDB entries  
EC 3.-.-.- Hydrolases. [21,051 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,852 PDB entries]
EC 3.4.24.- Metalloendopeptidases. [610 PDB entries]
EC 3.4.24.21 Astacin. [9 PDB entries]    
1ast

Reaction: Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
Other name(s): Astacus proteinase. Crayfish small-molecule proteinase.
Cofactor(s): Zn(2+).
Comments: A digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis. Belongs to peptidase family M12A. Formerly Ec 3.4.99.6.
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There are 9 PDB entries in enzyme class E.C.3.4.24.21

  PDB code Protein
1ast
Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1iaa
Crystal structures, spectroscopic features, and catalytic properties of cobalt(ii), copper(ii), nickel(ii), and mercury(ii) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1iab
Crystal structures, spectroscopic features, and catalytic properties of cobalt(ii), copper(ii), nickel(ii), and mercury(ii) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1iac
Refined 1.8 angstroms x-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish astacus astacus l. Structure determination, refinement, molecular structure and comparison with thermolysin
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1iad
Refined 1.8 angstroms x-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish astacus astacus l. Structure determination, refinement, molecular structure and comparison to thermolysin
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1iae
Crystal structures, spectroscopic features, and catalytic properties of cobalt(ii), copper(ii), nickel(ii), and mercury(ii) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715
Chain: A (200 residues) CATH domain: 3.40.390.10
1qji
Structure of astacin with a transition-state analogue inhibitor
Source: Astacus fluviatilis. Broad-fingered crayfish. Organism_taxid: 6715. Organ: midgut gland. Cell: f-cell. Secretion: digestive fluid. Gene: astacin
Chain: A (200 residues) CATH domain: 3.40.390.10
1qjj
Structure of astacin with a hydroxamic acid inhibitor
Source: Astacus fluviatilis. Broad-fingered crayfish. Organism_taxid: 6715. Organ: midgut gland. Cell: f-cell. Secretion: digestive fluid. Synthetic: yes
Chain: A (200 residues) CATH domain: 3.40.390.10
3lq0
Zymogen structure of crayfish astacin metallopeptidase
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (235 residues) CATH domain: 3.40.390.10