4CJZ
Crystal structure of the integral membrane diacylglycerol kinase DgkA- 9.9, delta 4
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004143 | molecular_function | ATP-dependent diacylglycerol kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006654 | biological_process | phosphatidic acid biosynthetic process |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0008654 | biological_process | phospholipid biosynthetic process |
A | 0009411 | biological_process | response to UV |
A | 0016020 | cellular_component | membrane |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004143 | molecular_function | ATP-dependent diacylglycerol kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006654 | biological_process | phosphatidic acid biosynthetic process |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0008654 | biological_process | phospholipid biosynthetic process |
B | 0009411 | biological_process | response to UV |
B | 0016020 | cellular_component | membrane |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004143 | molecular_function | ATP-dependent diacylglycerol kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006654 | biological_process | phosphatidic acid biosynthetic process |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0008654 | biological_process | phospholipid biosynthetic process |
C | 0009411 | biological_process | response to UV |
C | 0016020 | cellular_component | membrane |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OLC C 1120 |
Chain | Residue |
B | ALA13 |
C | ALA30 |
C | GLN33 |
C | GLU69 |
C | ASN72 |
C | SER98 |
C | VAL101 |
C | ALA108 |
C | TRP112 |
Functional Information from PROSITE/UniProt
site_id | PS01069 |
Number of Residues | 12 |
Details | DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD |
Chain | Residue | Details |
A | GLU69-ASP80 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 87 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:8071224 |
Chain | Residue | Details |
A | ALA1-ALA30 | |
B | ALA1-ALA30 | |
C | ALA1-ALA30 |
site_id | SWS_FT_FI2 |
Number of Residues | 99 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 |
Chain | Residue | Details |
A | PHE31-TRP47 | |
A | ASP51-VAL68 | |
B | PHE31-TRP47 | |
B | ASP51-VAL68 | |
C | PHE31-TRP47 | |
C | ASP51-VAL68 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | TOPO_DOM: Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 |
Chain | Residue | Details |
A | LEU48-VAL50 | |
B | LEU48-VAL50 | |
C | LEU48-VAL50 |
site_id | SWS_FT_FI4 |
Number of Residues | 75 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:8071224 |
Chain | Residue | Details |
A | GLU69-LYS94 | |
B | GLU69-LYS94 | |
C | GLU69-LYS94 |
site_id | SWS_FT_FI5 |
Number of Residues | 69 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:8071224 |
Chain | Residue | Details |
A | ASP95-SER118 | |
B | ASP95-SER118 | |
C | ASP95-SER118 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224 |
Chain | Residue | Details |
A | HIS119-GLY121 | |
B | HIS119-GLY121 | |
C | HIS119-GLY121 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:26673816 |
Chain | Residue | Details |
A | GLU69 | |
B | GLU69 | |
C | GLU69 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538 |
Chain | Residue | Details |
A | ARG9 | |
B | ARG9 | |
C | ARG9 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 |
Chain | Residue | Details |
A | ALA13 | |
B | ALA13 | |
C | ALA13 |
site_id | SWS_FT_FI10 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 |
Chain | Residue | Details |
A | TYR16 | |
B | LYS94 | |
C | TYR16 | |
C | GLU28 | |
C | GLU76 | |
C | GLU85 | |
C | LYS94 | |
A | GLU28 | |
A | GLU76 | |
A | GLU85 | |
A | LYS94 | |
B | TYR16 | |
B | GLU28 | |
B | GLU76 | |
B | GLU85 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129 |
Chain | Residue | Details |
A | ARG22 | |
B | ARG22 | |
C | ARG22 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 |
Chain | Residue | Details |
A | ALA30 | |
B | ALA30 | |
C | ALA30 |
site_id | SWS_FT_FI13 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25 |
Chain | Residue | Details |
A | TRP47 | |
B | TRP47 | |
C | TRP47 |
site_id | SWS_FT_FI14 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25 |
Chain | Residue | Details |
A | ARG55 | |
B | ARG55 | |
C | ARG55 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26 |
Chain | Residue | Details |
A | GLU69 | |
B | GLU69 | |
C | GLU69 |
site_id | SWS_FT_FI16 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 |
Chain | Residue | Details |
A | SER98 | |
B | SER98 | |
C | SER98 |
site_id | SWS_FT_FI17 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26 |
Chain | Residue | Details |
A | TRP112 | |
B | TRP112 | |
C | TRP112 |