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1HI9

Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
B0004177molecular_functionaminopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0030435biological_processsporulation resulting in formation of a cellular spore
B0046872molecular_functionmetal ion binding
C0004177molecular_functionaminopeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0016787molecular_functionhydrolase activity
C0030435biological_processsporulation resulting in formation of a cellular spore
C0046872molecular_functionmetal ion binding
D0004177molecular_functionaminopeptidase activity
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0016787molecular_functionhydrolase activity
D0030435biological_processsporulation resulting in formation of a cellular spore
D0046872molecular_functionmetal ion binding
E0004177molecular_functionaminopeptidase activity
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
E0008237molecular_functionmetallopeptidase activity
E0016787molecular_functionhydrolase activity
E0030435biological_processsporulation resulting in formation of a cellular spore
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
AASP8
AHIS104
AHIS115
AGLU133
AZN301
AHOH2059

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AZN300
AHOH2059
AASP8
AGLU10
AHIS60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BASP8
BHIS104
BHIS115
BGLU133
BZN301
BHOH2025

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BASP8
BGLU10
BHIS60
BZN300
BHOH2025

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 300
ChainResidue
CASP8
CHIS104
CHIS115
CGLU133
CZN301
CHOH2037

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CASP8
CGLU10
CHIS60
CZN300
CHOH2037

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN D 300
ChainResidue
DASP8
DHIS104
DHIS115
DGLU133
DZN301
DHOH2053

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DASP8
DGLU10
DHIS60
DZN300
DHOH2053

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN E 300
ChainResidue
EASP8
EHIS104
EHIS115
EGLU133
EZN301
EHOH2073

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 301
ChainResidue
EASP8
EGLU10
EHIS60
EZN300
EHOH2073

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues25
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2026-01-28

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