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6YCC

Structure the ananain protease from Ananas comosus covalently bound to the E64 inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue E64 A 301
ChainResidue
AGLN19
ATRP66
AALA132
ALEU155
AASN156
AHIS157
AALA158
AHOH406
AHOH562
AGLY23
ASER24
ACYS25
ATRP26
ATYR60
ALYS63
AGLY64
AGLY65

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS39
AGLY43
AASN44
ALEU45
AHOH494
BLYS41

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 303
ChainResidue
ALYS17
AASN18
AGLU50
AHOH423
AHOH446
AHOH476
AHOH514

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLY61
ACYS62
ALYS92
AHOH402
AHOH420
AHOH512
AHOH527

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 B 302
ChainResidue
ALYS41
BLYS39
BGLY43
BASN44
BLEU45
BHOH508

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 303
ChainResidue
BGLY93
BTHR94
BHOH406

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL B 304
ChainResidue
BLYS17
BASN18
BGLU50
BHOH438
BHOH444
BHOH486
BHOH522

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 305
ChainResidue
ASER10
ALYS39
AILE40
BSER10
BALA12
BLYS39
BHOH422

site_idAC9
Number of Residues17
Detailsbinding site for Di-peptide E64 B 301 and CYS B 25
ChainResidue
BGLN19
BGLY23
BSER24
BTRP26
BALA27
BPHE28
BALA29
BTYR60
BLYS63
BGLY64
BGLY65
BALA132
BLEU155
BASN156
BHIS157
BALA158
BHOH414

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGrCGSCWAfAS
ChainResidueDetails
AGLN19-SER30

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHAIVIIGYG
ChainResidueDetails
ALEU155-GLY165

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. FWIvRNSWgagWGegGYIrL
ChainResidueDetails
APHE173-LEU192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31306685","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31306685","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"31306685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6MIS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6YCC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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