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Ligands
Code Name Style Show Link
MN Manganese (II) ion
Non-standard Residues
Code Name Show
01B (2s,3r)-3-amino-2-hydroxy-4-phenylbutanoic acid
Glycosylation
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Modification
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NH2 Amino group
Code : 6A9U   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal strcture of Icp55 from Saccharomyces cerevisiae bound to apstatin inhibitor
Release Data : 2019-01-16
Compound :
mol_id molecule chains synonym
1 Intermediate cleaving peptidase 55 A Intermediate cleaving peptidase of 55 kDa
ec: 3.4.11.26
mutation: D189E
mol_id molecule chains
2 apstatin B
Source :
mol_id organism_scientific organism_common expression_system
1 Saccharomyces cerevisiae S288c  (taxid:559292) Baker's yeast Escherichia coli  (taxid:562)
strain: ATCC 204508 / S288c
gene: ICP55, YER078C
expression_system_strain: BL21 (DE3)
expression_system_plasmid: pST50STR
mol_id organism_scientific
2 Synthetic construct  (taxid:3263)
synthetic: yes
Authors : Singh, R., Kumar, A., Goyal, V.D., Makde, R.D.
Keywords : Intermediate cleaving peptidase 55, M24B, peptidase, Xaa-Pro aminopeptidase, mitochondrial, Apstatin, N-((2S, 3R)-3-Amino-2-hydroxy-4-phenylbutanoyl)-Pro-Pro-Ala-NH2, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.400 Å )
Citation :

Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function.

Singh, R.,Goyal, V.D.,Kumar, A.  et al.
(2019)  FEBS Lett.  593 : 443 - 454

PubMed: 30582634
DOI: 10.1002/1873-3468.13321

Chain : A
UniProt : P40051 (ICP55_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser- Pro) from the N-terminus after cleavage by mitochondrial processing peptidase. 3.4.11.26 PubMed:19720832, PubMed:19837041
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