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2ZWO

Crystal structure of Ca2 site mutant of Pro-S324A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0042802molecular_functionidentical protein binding
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0042802molecular_functionidentical protein binding
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
C0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 399
ChainResidue
AGLN84
AASP124
ALEU164
AASN166
AILE168
AVAL170

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AILE218
AASP222
AASP225
AASP212
AASP214
AASP216

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP214
AASP216
AASP222
AASP224
AHOH607

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AVAL108
AGLN110
AALA227
AGLU229
AHOH447
AHOH580

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP119
AASP121
AASP314
AASP315
AHOH604

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AASP372
ALEU373
APRO375
AGLY377
AASP379
AHOH560

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 399
ChainResidue
BGLN84
BASP124
BLEU164
BASN166
BILE168
BVAL170

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 400
ChainResidue
BASP212
BASP214
BASP216
BILE218
BASP222
BASP225

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
ATHR142
AHOH438
BASP214
BASP216
BASP222
BASP224

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASP372
BLEU373
BPRO375
BGLY377
BASP379

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BVAL108
BGLN110
BALA227
BGLU229
BHOH433
BHOH651

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 399
ChainResidue
CGLN84
CASP124
CLEU164
CASN166
CILE168
CVAL170

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 400
ChainResidue
CASP212
CASP214
CASP216
CILE218
CASP222
CASP225

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 401
ChainResidue
CASP214
CASP216
CASP222
CHOH533

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 402
ChainResidue
CASP372
CLEU373
CPRO375
CGLY377
CASP379
CHOH486

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 403
ChainResidue
CVAL108
CGLN110
CALA227
CGLU229
CHOH521
CHOH544

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 Residues9
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP115
AHIS153
AALA324
BASP115
BHIS153
BALA324
CASP115
CHIS153
CALA324

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PDB entries from 2024-05-01

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