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3DLJ

Crystal structure of human carnosine dipeptidase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0051246biological_processregulation of protein metabolic process
A0070573molecular_functionmetallodipeptidase activity
B0004180molecular_functioncarboxypeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
B0046872molecular_functionmetal ion binding
B0051246biological_processregulation of protein metabolic process
B0070573molecular_functionmetallodipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 2001
ChainResidue
AASP139
AGLU174
AHIS452
AZN2002
AUNX2004

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 2002
ChainResidue
AZN2001
AUNX2004
AHIS106
AASP139
AGLU173
AASP202

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 2004
ChainResidue
AGLU173
AASP202
AZN2001
AZN2002

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 2006
ChainResidue
AHIS235
ATHR337
BARG350
BHIS452

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 2007
ChainResidue
AASP331
AGLU332

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 2008
ChainResidue
AVAL41
AARG43

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 2009
ChainResidue
AARG43

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 2010
ChainResidue
BARG299

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 2011
ChainResidue
AALA248
AALA252
BHOH2040

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 2012
ChainResidue
ALEU243
AHIS244
AGLU245
AALA248

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
AARG299
BARG230
BASP231
BGLN232

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2001
ChainResidue
BASP139
BGLU174
BHIS452
BZN2002
BUNX2003

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 2002
ChainResidue
BHIS106
BASP139
BGLU173
BASP202
BZN2001
BUNX2003

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 2003
ChainResidue
AHIS235
BZN2001
BZN2002

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 2004
ChainResidue
BASP331
BGLU332
BHOH2027

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX B 2005
ChainResidue
BPRO353
BPRO391

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 2006
ChainResidue
BMET224
BVAL382
BSER384

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 2007
ChainResidue
BPHE23
BTHR26
BASN149

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX B 2008
ChainResidue
BCYS229

Functional Information from PROSITE/UniProt
site_idPS00759
Number of Residues40
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. ATDnKGpvLawInavsafraleqdlpvn.IkFIIegMEEaG
ChainResidueDetails
AALA137-GLY176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP108
BASP108

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU173
BGLU173

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|Ref.11
ChainResidueDetails
AHIS106
BHIS452
AASP139
AGLU174
AASP202
AHIS452
BHIS106
BASP139
BGLU174
BASP202

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HG3
ChainResidueDetails
ASER193
BSER193

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN296
AASN356
BASN296
BASN356

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLU173

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLU173

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PDB entries from 2024-09-04

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