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6M8W

PSEUDOMONAS SERINE-CARBOXYL PROTEINASE (SEDOLISIN) COMPLEXED WITH THE INHIBITOR AIAF

Replaces:  1KDV
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 401
ChainResidue
AASP328
AVAL329
AGLY344
AGLY346
AASP348
AHOH637

site_idAC2
Number of Residues11
Detailsbinding site for residue GOL A 402
ChainResidue
ATHR186
ALEU273
ATYR275
ALEU280
AHOH503
AHOH536
AHOH548
AHOH714
AASN9
APHE48
AASN52

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
AALA5
AASN221
AGLU222
AHOH561
AHOH578

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
AHOH710
AHOH735
AHOH923
AHOH927

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 401
ChainResidue
AGLY77
BACE381
BILE382
BALA383
BHOH502
BHOH503
BHOH504
BHOH506

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_idMCSA1
Number of Residues4
DetailsM-CSA 380
ChainResidueDetails
AGLU80proton shuttle (general acid/base)
AASP84proton shuttle (general acid/base)
AASP170electrostatic stabiliser
ASER287covalent catalysis

218853

PDB entries from 2024-04-24

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