Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion
PBZ P-amino benzamidine
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose
BMA Beta-D-mannopyranose
FUL Beta-L-fucopyranose
Modification
Code Name Show
Code : 1FIZ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA
Release Data : 2000-11-08
Compound :
mol_id molecule chains
1 BETA-ACROSIN HEAVY CHAIN A
mol_id molecule chains
2 BETA-ACROSIN LIGHT CHAIN L
Source :
mol_id organism_scientific organism_common
1 Sus scrofa  (taxid:9823) Pig
organ: TESTIS
cell: SPERMATOZOA
mol_id organism_scientific organism_common
2 Sus scrofa  (taxid:9823) Pig
organ: TESTIS
cell: SPERMATOZOA
Authors : Tranter, R., Read, J.A., Jones, R., Brady, R.L.
Keywords : anti-parallel beta-barrel, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.9 Å )
Citation :

Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin.

Tranter, R.,Read, J.A.,Jones, R.  et al.
(2000)  Structure Fold.Des.  8 : 1179 - 1188

PubMed: 11080640
DOI: 10.1016/S0969-2126(00)00523-2

Three dimensional structure of beta-acrosin from ram and boar spermatozoa

Tranter, R.
Thesis 

Chain : L
UniProt : P08001 (ACRO_PIG)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. 3.4.21.10 -
-