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1GA6

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 374
ChainResidue
AASP328
AVAL329
AGLY344
AGLY346
AASP348
AHOH401

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 395
ChainResidue
AGLY169
AGLU171
AARG179
ASER287
AHOH486
ALEU134
AGLY135
ASER167

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 396
ChainResidue
ATHR24
APRO196
APRO244
AHOH417
AHOH461
AHOH480

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 397
ChainResidue
ALYS128
AGLY161
ASER307
ALEU308
AGLY309
AGOL392
AHOH635

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 398
ChainResidue
ASER324
AVAL326
AHIS327
AASP357
ALYS360

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 391
ChainResidue
AASN9
APHE48
AASN52
ATHR186
ALEU273
ATYR275
ALEU280
AHOH434
AHOH489
AHOH515
AHOH564
AHOH866

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 392
ChainResidue
ASER20
AGLY309
ASER314
APHE370
AACT397
AHOH414
AHOH424
AHOH437
AHOH444
AHOH459
AHOH460

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 393
ChainResidue
AASN125
AVAL126
AASN306
AHOH465
AHOH484
AHOH680
AHOH751

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 394
ChainResidue
AALA5
AASN221
AGLU222
AHOH421
AHOH651

Functional Information from PROSITE/UniProt
site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAsPiFVG
ChainResidueDetails
AGLY285-GLY295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:10488127
ChainResidueDetails
AGLU80
AASP84
ASER287

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AASP328
AVAL329
AGLY344
AGLY346
AASP348

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1nlu
ChainResidueDetails
AGLU80
AASP170
ASER287
AASP84

site_idMCSA1
Number of Residues4
DetailsM-CSA 380
ChainResidueDetails
AGLU80proton shuttle (general acid/base)
AASP84proton shuttle (general acid/base)
AASP170electrostatic stabiliser
ASER287covalent catalysis

223532

PDB entries from 2024-08-07

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