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5NIJ

Crystal structure of arabidopsis thaliana legumain isoform gamma in two-chain activation state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000323cellular_componentlytic vacuole
A0000326cellular_componentprotein storage vacuole
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005773cellular_componentvacuole
A0006508biological_processproteolysis
A0006624biological_processvacuolar protein processing
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009611biological_processresponse to wounding
A0009723biological_processresponse to ethylene
A0009751biological_processresponse to salicylic acid
A0009753biological_processresponse to jasmonic acid
A0010150biological_processleaf senescence
A0051603biological_processproteolysis involved in protein catabolic process
B0000323cellular_componentlytic vacuole
B0000326cellular_componentprotein storage vacuole
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005773cellular_componentvacuole
B0006508biological_processproteolysis
B0006624biological_processvacuolar protein processing
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0009611biological_processresponse to wounding
B0009723biological_processresponse to ethylene
B0009751biological_processresponse to salicylic acid
B0009753biological_processresponse to jasmonic acid
B0010150biological_processleaf senescence
B0051603biological_processproteolysis involved in protein catabolic process
C0000323cellular_componentlytic vacuole
C0000326cellular_componentprotein storage vacuole
C0004175molecular_functionendopeptidase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0005773cellular_componentvacuole
C0006508biological_processproteolysis
C0006624biological_processvacuolar protein processing
C0008233molecular_functionpeptidase activity
C0008234molecular_functioncysteine-type peptidase activity
C0009611biological_processresponse to wounding
C0009723biological_processresponse to ethylene
C0009751biological_processresponse to salicylic acid
C0009753biological_processresponse to jasmonic acid
C0010150biological_processleaf senescence
C0051603biological_processproteolysis involved in protein catabolic process
D0000323cellular_componentlytic vacuole
D0000326cellular_componentprotein storage vacuole
D0004175molecular_functionendopeptidase activity
D0004197molecular_functioncysteine-type endopeptidase activity
D0005773cellular_componentvacuole
D0006508biological_processproteolysis
D0006624biological_processvacuolar protein processing
D0008233molecular_functionpeptidase activity
D0008234molecular_functioncysteine-type peptidase activity
D0009611biological_processresponse to wounding
D0009723biological_processresponse to ethylene
D0009751biological_processresponse to salicylic acid
D0009753biological_processresponse to jasmonic acid
D0010150biological_processleaf senescence
D0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 501
ChainResidue
AHIS310
CALA374

site_idAC2
Number of Residues8
Detailsbinding site for residue CIT A 502
ChainResidue
ATRP485
AASN72
AHIS177
AASP358
AARG390
ASER446
AGLN447
ATYR448

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 B 501
ChainResidue
BSER373
BALA374
DLYS297

site_idAC4
Number of Residues1
Detailsbinding site for residue SO4 B 502
ChainResidue
BARG87

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 C 501
ChainResidue
CSER119
CPRO120
CHIS121
CGLY122

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 D 501
ChainResidue
DSER119
DHIS121
DGLY122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O89017
ChainResidueDetails
AHIS177
BHIS177
CHIS177
DHIS177

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O89017
ChainResidueDetails
ASCH219
BSCH219
CSCH219
DSCH219

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Required for post-translational maturation and enzyme activity => ECO:0000250|UniProtKB:Q84LM2
ChainResidueDetails
ACYS266
BCYS266
CCYS266
DCYS266

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN336
BASN336
CASN336
DASN336

220472

PDB entries from 2024-05-29

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