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 | 0006880 | biological_process | intracellular sequestering of iron ion |
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 | 0006880 | biological_process | intracellular sequestering of iron ion |
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 | 0006880 | biological_process | intracellular sequestering of iron ion |
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 | 0006880 | biological_process | intracellular sequestering of iron ion |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR147 | |
B | TYR147 | |
C | TYR147 | |
D | TYR147 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16380372, ECO:0007744|PDB:2AG5 |
Chain | Residue | Details |
A | GLN16 | |
B | VAL180 | |
C | GLN16 | |
C | ASP37 | |
C | ASP58 | |
C | LYS151 | |
C | VAL180 | |
D | GLN16 | |
D | ASP37 | |
D | ASP58 | |
D | LYS151 | |
A | ASP37 | |
D | VAL180 | |
A | ASP58 | |
A | LYS151 | |
A | VAL180 | |
B | GLN16 | |
B | ASP37 | |
B | ASP58 | |
B | LYS151 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ARG144 | |
D | ARG144 | |
D | ARG188 | |
D | ARG205 | |
A | ARG188 | |
A | ARG205 | |
B | ARG144 | |
B | ARG188 | |
B | ARG205 | |
C | ARG144 | |
C | ARG188 | |
C | ARG205 |
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 |