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1NLU

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

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 501
ChainResidue
AASP328
AVAL329
AGLY344
AGLY346
AASP348
AHOH502

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN
ChainResidue
ASER133
ALEU134
AGLY135
ATRP136
AGLY169
AASP170
AGLU171
AGLU175
AARG179
ASER190
AGLY285
ATHR286
ASER287
AHOH736
BHOH182
AASP74
AGLU80
ATRP81

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN
ChainResidue
AGLY79
AGLU80
AGLU222
ATRP231
AGLN268
AGLN281
AILE283
AGLY284
AHOH908
CHOH152
CHOH288
CHOH360
CHOH380
CHOH442

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

218500

PDB entries from 2024-04-17

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