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1EB6

Deuterolysin from Aspergillus oryzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 178
ChainResidue
AHIS128
AHIS132
AASP143
AHOH2255
AHOH2256

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A1178
ChainResidue
AHOH2257
AHOH2258
AASP9
ASER12
ASER13
ASER96

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A1179
ChainResidue
AHIS118
AALA119
AGLN120
ATHR124
AALA167
ALEU168
AASN171
AHOH2238

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1180
ChainResidue
AALA114
AASP121
ATHR124
AASN171
AHOH2259

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TTLHEFTHAP
ChainResidueDetails
ATHR125-PRO134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11679721
ChainResidueDetails
AGLU129

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11679721, ECO:0007744|PDB:1EB6
ChainResidueDetails
AHIS128
AHIS132
AASP143

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10446194, 11679721
ChainResidueDetails
ATYR106
AGLU129

site_idMCSA1
Number of Residues5
DetailsM-CSA 596
ChainResidueDetails
ATYR106electrostatic stabiliser
AHIS128metal ligand
AGLU129electrostatic stabiliser
AHIS132metal ligand
AASP143metal ligand

223790

PDB entries from 2024-08-14

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