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3P8F

Crystal Structure of MT-SP1 in complex with SFTI-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GSH A 1001
ChainResidue
AARG119
APRO120
ACYS122
AILE207

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR CHAIN I OF TRYPSIN INHIBITOR 1
ChainResidue
APHE97
APHE99
AASP125
AGLN175
ASER190
ACYS191
AGLN192
AGLY193
AASP194
ASER195
APHE208
ASER214
ATRP215
AGLY216
AASP217
AILE41
ACYS42
AHIS57
AARG60
ATYR60

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS
ChainResidueDetails
AASP189-SER200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN164
IASP14

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PDB entries from 2024-07-24

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