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2ID4

The 1.9 A structure of Kex2 in complex with an Ac-R-E-R-K-chloromethyl ketone inhibitor.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AAIVDDGLdyeN
ChainResidueDetails
AALA171-ASN182

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeIAA
ChainResidueDetails
AHIS213-ALA223

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaAaPlAAG
ChainResidueDetails
AGLY383-GLY393

site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VTVDIDT
ChainResidueDetails
AVAL510-THR516

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP175
AHIS213
ASER385
BASP175
BHIS213
BSER385

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP135
BASP277
BASP320
BGLU350
AASP184
AASN227
AASP277
AASP320
AGLU350
BASP135
BASP184
BASN227

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN163
AASN480
BASN163
BASN480

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN404
BASN404

220113

PDB entries from 2024-05-22

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