4RUH
Crystal structure of Human Carnosinase-2 (CN2) in complex with inhibitor, Bestatin at 2.25 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0070062 | cellular_component | extracellular exosome |
| A | 0070573 | molecular_function | metallodipeptidase activity |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0070062 | cellular_component | extracellular exosome |
| B | 0070573 | molecular_function | metallodipeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BES A 501 |
| Chain | Residue |
| A | HIS99 |
| A | SER417 |
| A | HIS445 |
| A | MN502 |
| A | MN503 |
| B | HIS228 |
| B | VAL231 |
| B | THR330 |
| A | ASP132 |
| A | GLU166 |
| A | GLU167 |
| A | ASP195 |
| A | ARG343 |
| A | HIS380 |
| A | GLU414 |
| A | GLY416 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 502 |
| Chain | Residue |
| A | HIS99 |
| A | ASP132 |
| A | GLU167 |
| A | ASP195 |
| A | BES501 |
| A | MN503 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 503 |
| Chain | Residue |
| A | ASP132 |
| A | GLU167 |
| A | HIS445 |
| A | BES501 |
| A | MN502 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BES B 501 |
| Chain | Residue |
| A | HIS228 |
| A | VAL231 |
| A | THR330 |
| B | HIS99 |
| B | ASP132 |
| B | GLU166 |
| B | GLU167 |
| B | ASP195 |
| B | ASN196 |
| B | TYR197 |
| B | ARG343 |
| B | GLU414 |
| B | GLY416 |
| B | SER417 |
| B | ILE418 |
| B | HIS445 |
| B | MN502 |
| B | MN503 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 502 |
| Chain | Residue |
| B | HIS99 |
| B | ASP132 |
| B | GLU166 |
| B | ASP195 |
| B | BES501 |
| B | MN503 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 503 |
| Chain | Residue |
| B | ASP132 |
| B | GLU167 |
| B | HIS445 |
| B | BES501 |
| B | MN502 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | ASP226 |
| B | GLY321 |
| B | ALA322 |
| B | PHE323 |
| B | LYS329 |
| B | VAL331 |
| B | PRO333 |
| B | HOH684 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 505 |
| Chain | Residue |
| B | LYS181 |
| B | PHE185 |
| B | LYS186 |
| B | VAL188 |
| B | THR428 |
| B | LYS430 |
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. STDdKGpvAgwInaleayqktgqeipvn.VrFCLegMEEsG |
| Chain | Residue | Details |
| A | SER130-GLY169 |
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 | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of Human Carnosinase-2 (CN2) in complex with inhibitor, Bestatin at 2.25 A.","authors":["Pandya V.","Kaushik A.","Singh A.K.","Singh R.P.","Kumaran S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6Q0N1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
