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2E1P

Crystal structure of pro-Tk-subtilisin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP226
AHOH1267
AHOH1275
ALEU205
AASP208
AVAL210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP212
AASP214
AASP216
AILE218
AASP222
AASP225

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP214
AASP216
AASP222
AASP224
AHOH1058

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH1007
AHOH1092

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1006
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH1023

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGVdydH
ChainResidueDetails
AVAL111-HIS122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues306
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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