1TEV
Crystal structure of the human UMP/CMP kinase in open conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004127 | molecular_function | (d)CMP kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0004849 | molecular_function | uridine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006222 | biological_process | UMP biosynthetic process |
| A | 0006225 | biological_process | UDP biosynthetic process |
| A | 0009041 | molecular_function | UMP/dUMP kinase activity |
| A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0033862 | molecular_function | UMP kinase activity |
| A | 0036430 | molecular_function | CMP kinase activity |
| A | 0036431 | molecular_function | dCMP kinase activity |
| A | 0046705 | biological_process | CDP biosynthetic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072528 | biological_process | pyrimidine-containing compound biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | GLY11 |
| A | GLY13 |
| A | ALA14 |
| A | GLY15 |
| A | LYS16 |
| A | GLY17 |
| A | ARG134 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLIDGFPRnqdN |
| Chain | Residue | Details |
| A | PHE89-ASN100 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03172 |
| Chain | Residue | Details |
| A | GLY13 | |
| A | ARG39 | |
| A | LYS61 | |
| A | GLY93 | |
| A | ASN100 | |
| A | ARG134 | |
| A | ARG140 | |
| A | ARG151 | |
| A | LYS179 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER33 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBP5 |
| Chain | Residue | Details |
| A | LYS43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS55 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBP5 |
| Chain | Residue | Details |
| A | LYS106 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q4KM73 |
| Chain | Residue | Details |
| A | SER180 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS73 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | ASP142 | |
| A | ARG151 | |
| A | ARG140 | |
| A | ASP143 | |
| A | ARG134 | |
| A | LYS16 |
