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1AEC

CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE E64 A 219
ChainResidue
AGLN19
AGLY68
ATYR69
AASN88
AASP161
AHIS162
AHOH272
AHOH305
AHOH481
AHOH485
AGLY23
AGLY24
ACYS25
ATRP26
AASN61
AARG63
AASN66
AGLY67

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGeCGGCWAfSA
ChainResidueDetails
AGLN19-ALA30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. IDHAVTIVGYG
ChainResidueDetails
AILE160-GLY170

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWdttWGeeGYMrI
ChainResidueDetails
ATYR177-ILE196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000305|PubMed:1606141, ECO:0007744|PDB:1AEC
ChainResidueDetails
ACYS25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089
ChainResidueDetails
AHIS162

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090
ChainResidueDetails
AASN182

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: covalent => ECO:0000269|PubMed:1606141, ECO:0007744|PDB:1AEC
ChainResidueDetails
ACYS25

218853

PDB entries from 2024-04-24

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