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1POK

Crystal structure of Isoaspartyl Dipeptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
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
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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 391
ChainResidue
BHIS70
BGLY74
BGLY75
BGLU77
BTHR106
BTYR137
BSER289
BASN401
BZN603

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 603
ChainResidue
BHIS68
BHIS70
BKCX162
BASP285
BSO4391
BASN401
BZN604

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 604
ChainResidue
BTYR137
BKCX162
BHIS201
BHIS230
BASN401
BZN603

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 391
ChainResidue
AHIS70
AGLY74
AGLY75
AGLU77
AGLY105
ATHR106
ATYR137
ASER289
AHOH616

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AHIS68
AHIS70
AKCX162
AASP285
AZN602

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 602
ChainResidue
ATYR137
AKCX162
AHIS201
AHIS230
AASN400
AZN601

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ASN B 401
ChainResidue
BTYR137
BARG169
BHIS201
BHIS230
BARG233
BASP285
BSER289
BSO4391
BZN603
BZN604

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ASN A 400
ChainResidue
ATYR137
AARG169
AHIS201
AARG233
AASP285
AZN602

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

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
BHIS68
AASP285
BHIS70
BHIS201
BHIS230
BASP285
AHIS68
AHIS70
AHIS201
AHIS230

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
BGLY75
AGLY75

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

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
BKCX162
AKCX162

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
BKCX162
AKCX162

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 172
ChainResidueDetails
BHIS68metal ligand
BHIS70metal ligand
BKCX162metal ligand
BHIS201metal ligand
BHIS230metal ligand
BASP285hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 172
ChainResidueDetails
AHIS68metal ligand
AHIS70metal ligand
AKCX162metal ligand
AHIS201metal ligand
AHIS230metal ligand
AASP285hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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PDB entries from 2024-09-11

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