3DLJ
Crystal structure of human carnosine dipeptidase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051246 | biological_process | regulation of protein metabolic process |
| A | 0070573 | molecular_function | metallodipeptidase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016805 | molecular_function | dipeptidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051246 | biological_process | regulation of protein metabolic process |
| B | 0070573 | molecular_function | metallodipeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 2001 |
| Chain | Residue |
| A | ASP139 |
| A | GLU174 |
| A | HIS452 |
| A | ZN2002 |
| A | UNX2004 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 2002 |
| Chain | Residue |
| A | ZN2001 |
| A | UNX2004 |
| A | HIS106 |
| A | ASP139 |
| A | GLU173 |
| A | ASP202 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 2004 |
| Chain | Residue |
| A | GLU173 |
| A | ASP202 |
| A | ZN2001 |
| A | ZN2002 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 2006 |
| Chain | Residue |
| A | HIS235 |
| A | THR337 |
| B | ARG350 |
| B | HIS452 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 2007 |
| Chain | Residue |
| A | ASP331 |
| A | GLU332 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 2008 |
| Chain | Residue |
| A | VAL41 |
| A | ARG43 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 2009 |
| Chain | Residue |
| A | ARG43 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 2010 |
| Chain | Residue |
| B | ARG299 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 2011 |
| Chain | Residue |
| A | ALA248 |
| A | ALA252 |
| B | HOH2040 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 2012 |
| Chain | Residue |
| A | LEU243 |
| A | HIS244 |
| A | GLU245 |
| A | ALA248 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2003 |
| Chain | Residue |
| A | ARG299 |
| B | ARG230 |
| B | ASP231 |
| B | GLN232 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | ASP139 |
| B | GLU174 |
| B | HIS452 |
| B | ZN2002 |
| B | UNX2003 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 2002 |
| Chain | Residue |
| B | HIS106 |
| B | ASP139 |
| B | GLU173 |
| B | ASP202 |
| B | ZN2001 |
| B | UNX2003 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 2003 |
| Chain | Residue |
| A | HIS235 |
| B | ZN2001 |
| B | ZN2002 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 2004 |
| Chain | Residue |
| B | ASP331 |
| B | GLU332 |
| B | HOH2027 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 2005 |
| Chain | Residue |
| B | PRO353 |
| B | PRO391 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 2006 |
| Chain | Residue |
| B | MET224 |
| B | VAL382 |
| B | SER384 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 2007 |
| Chain | Residue |
| B | PHE23 |
| B | THR26 |
| B | ASN149 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 2008 |
| Chain | Residue |
| B | CYS229 |
Functional Information from PROSITE/UniProt
| site_id | PS00759 |
| Number of Residues | 40 |
| Details | ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. ATDnKGpvLawInavsafraleqdlpvn.IkFIIegMEEaG |
| Chain | Residue | Details |
| A | ALA137-GLY176 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human carnosine dipeptidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66HG3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU173 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLU173 |
