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2AQO

Crystal structure of E. coli Isoaspartyl Dipeptidase Mutant E77Q

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008798molecular_functionbeta-aspartyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0008798molecular_functionbeta-aspartyl-peptidase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
AHIS68
AHIS70
AKCX162
AASP285
AZN802
AHOH1009

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 802
ChainResidue
AHIS230
AZN801
AHOH1009
ATYR137
AKCX162
AHIS201

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 803
ChainResidue
BHIS68
BHIS70
BKCX162
BASP285
BZN804
BHOH880

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 804
ChainResidue
BTYR137
BKCX162
BHIS201
BHIS230
BZN803
BHOH880

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:12946361
ChainResidueDetails
AASP285
BASP285

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685
ChainResidueDetails
AHIS68
BASP285
AHIS70
AHIS201
AHIS230
AASP285
BHIS68
BHIS70
BHIS201
BHIS230

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY75
BGLY75

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050
ChainResidueDetails
ATHR106
BSER289
ATYR137
AARG169
AARG233
ASER289
BTHR106
BTYR137
BARG169
BARG233

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685
ChainResidueDetails
AKCX162
BKCX162

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685
ChainResidueDetails
AKCX162
BKCX162

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 172
ChainResidueDetails
AHIS68metal ligand
AHIS70metal ligand
AKCX162metal ligand
ASER205metal ligand
AASN234metal ligand
ASER289hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 172
ChainResidueDetails
BHIS68metal ligand
BHIS70metal ligand
BKCX162metal ligand
BSER205metal ligand
BASN234metal ligand
BSER289hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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PDB entries from 2025-07-02

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