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1ELG

NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 280
ChainResidue
AGLU74
AASN76
AGLN79
AASN81
AGLU84
AHOH327

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BAA A 256
ChainResidue
ATHR44
ACYS45
AHIS60
AGLY201
ASER203
AHOH446
AHOH731
AHOH972

site_idCAT
Number of Residues3
Details
ChainResidue
AASP108
AHIS60
ASER203

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MTAAHC
ChainResidueDetails
AMET56-CYS61

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SGcqGDSGGPLH
ChainResidueDetails
ASER197-HIS208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:5415110
ChainResidueDetails
AHIS60

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110
ChainResidueDetails
AASP108
ASER203

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7656008, ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC
ChainResidueDetails
AGLU74
AASN76
AGLN79
AGLU84

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY204
ASER203

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY201
ASER203

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS60
ASER203
AASP108

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY204
AHIS60
ASER203
AASP108

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY201
AHIS60
ASER203
AASP108

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS60
AASP108

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY201
AHIS60
ASER222
ASER203
AASP108

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PDB entries from 2024-07-10

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