2AG5
Crystal Structure of Human DHRS6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016617 | molecular_function | 4-oxoproline reductase activity |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0019290 | biological_process | siderophore biosynthetic process |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0042168 | biological_process | heme metabolic process |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016617 | molecular_function | 4-oxoproline reductase activity |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0019290 | biological_process | siderophore biosynthetic process |
| B | 0030855 | biological_process | epithelial cell differentiation |
| B | 0042168 | biological_process | heme metabolic process |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070062 | cellular_component | extracellular exosome |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016617 | molecular_function | 4-oxoproline reductase activity |
| C | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| C | 0019290 | biological_process | siderophore biosynthetic process |
| C | 0030855 | biological_process | epithelial cell differentiation |
| C | 0042168 | biological_process | heme metabolic process |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016617 | molecular_function | 4-oxoproline reductase activity |
| D | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| D | 0019290 | biological_process | siderophore biosynthetic process |
| D | 0030855 | biological_process | epithelial cell differentiation |
| D | 0042168 | biological_process | heme metabolic process |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 5001 |
| Chain | Residue |
| A | ARG144 |
| A | LEU185 |
| A | ARG188 |
| A | PHE202 |
| A | ARG205 |
| A | NAD2001 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 5002 |
| Chain | Residue |
| C | PHE202 |
| C | ARG205 |
| C | NAD3001 |
| C | ARG144 |
| C | LEU185 |
| C | ARG188 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 5003 |
| Chain | Residue |
| B | ARG144 |
| B | LEU185 |
| B | ARG188 |
| B | PHE202 |
| B | NAD1001 |
| B | HOH5125 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 5004 |
| Chain | Residue |
| D | ARG144 |
| D | LEU185 |
| D | ARG188 |
| D | PHE202 |
| D | ARG205 |
| D | NAD4001 |
| D | HOH5166 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 1001 |
| Chain | Residue |
| B | ALA13 |
| B | ALA15 |
| B | GLN16 |
| B | GLY17 |
| B | ILE18 |
| B | ASP37 |
| B | ILE38 |
| B | LEU57 |
| B | ASP58 |
| B | VAL59 |
| B | VAL81 |
| B | GLY83 |
| B | LEU104 |
| B | SER132 |
| B | TYR147 |
| B | LYS151 |
| B | PRO177 |
| B | GLY178 |
| B | VAL180 |
| B | THR182 |
| B | PRO183 |
| B | SER184 |
| B | SO45003 |
| B | HOH5024 |
| B | HOH5123 |
| B | HOH5128 |
| B | HOH5133 |
| B | HOH5144 |
| B | HOH5174 |
| B | HOH5187 |
| B | HOH5191 |
| site_id | AC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 2001 |
| Chain | Residue |
| A | ALA13 |
| A | GLN16 |
| A | GLY17 |
| A | ILE18 |
| A | ASP37 |
| A | ILE38 |
| A | LEU57 |
| A | ASP58 |
| A | VAL59 |
| A | VAL81 |
| A | GLY83 |
| A | LEU104 |
| A | SER132 |
| A | TYR147 |
| A | LYS151 |
| A | PRO177 |
| A | GLY178 |
| A | VAL180 |
| A | THR182 |
| A | PRO183 |
| A | SER184 |
| A | SO45001 |
| A | HOH5012 |
| A | HOH5030 |
| A | HOH5088 |
| A | HOH5094 |
| A | HOH5100 |
| A | HOH5117 |
| A | HOH5120 |
| A | HOH5144 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD C 3001 |
| Chain | Residue |
| C | SER132 |
| C | TYR147 |
| C | LYS151 |
| C | PRO177 |
| C | GLY178 |
| C | THR179 |
| C | VAL180 |
| C | THR182 |
| C | PRO183 |
| C | SER184 |
| C | ARG188 |
| C | SO45002 |
| C | HOH5023 |
| C | HOH5033 |
| C | HOH5103 |
| C | HOH5122 |
| C | HOH5126 |
| C | HOH5139 |
| C | HOH5145 |
| C | HOH5174 |
| C | ALA13 |
| C | ALA15 |
| C | GLN16 |
| C | GLY17 |
| C | ILE18 |
| C | ASP37 |
| C | ILE38 |
| C | LEU57 |
| C | ASP58 |
| C | VAL59 |
| C | VAL81 |
| C | GLY83 |
| C | LEU104 |
| site_id | AC8 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD D 4001 |
| Chain | Residue |
| D | ALA13 |
| D | ALA15 |
| D | GLN16 |
| D | GLY17 |
| D | ILE18 |
| D | ASP37 |
| D | ILE38 |
| D | LEU57 |
| D | ASP58 |
| D | VAL59 |
| D | VAL81 |
| D | ALA82 |
| D | GLY83 |
| D | LEU104 |
| D | SER132 |
| D | TYR147 |
| D | LYS151 |
| D | PRO177 |
| D | GLY178 |
| D | THR179 |
| D | VAL180 |
| D | THR182 |
| D | PRO183 |
| D | SER184 |
| D | ARG188 |
| D | SO45004 |
| D | HOH5028 |
| D | HOH5035 |
| D | HOH5066 |
| D | HOH5082 |
| D | HOH5124 |
| D | HOH5128 |
| D | HOH5139 |
| D | HOH5169 |
| D | HOH5192 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. VassvkgvvnRcvYSTTKAAViGLTkSVA |
| Chain | Residue | Details |
| A | VAL134-ALA162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16380372","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AG5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | VAL138 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS151 | |
| A | ARG144 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS151 | |
| B | ARG144 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS151 | |
| C | ARG144 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS151 | |
| D | ARG144 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS151 | |
| A | TYR147 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS151 | |
| B | TYR147 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS151 | |
| C | TYR147 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS151 | |
| D | TYR147 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER133 | |
| A | LYS151 | |
| A | TYR147 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER133 | |
| B | LYS151 | |
| B | TYR147 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER133 | |
| C | LYS151 | |
| C | TYR147 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER133 | |
| D | LYS151 | |
| D | TYR147 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER133 | |
| A | LYS151 | |
| A | TYR147 | |
| A | ASN105 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER133 | |
| B | LYS151 | |
| B | TYR147 | |
| B | ASN105 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER133 | |
| C | LYS151 | |
| C | TYR147 | |
| C | ASN105 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER133 | |
| D | LYS151 | |
| D | TYR147 | |
| D | ASN105 |
