5TEJ
Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Vibrio vulnificus with 2,5 Furan Dicarboxylic and NADH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
A | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
B | 0019877 | biological_process | diaminopimelate biosynthetic process |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
C | 0009085 | biological_process | lysine biosynthetic process |
C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
C | 0019877 | biological_process | diaminopimelate biosynthetic process |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
D | 0009085 | biological_process | lysine biosynthetic process |
D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
D | 0019877 | biological_process | diaminopimelate biosynthetic process |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue NAD A 301 |
Chain | Residue |
A | GLY8 |
A | SER80 |
A | GLY98 |
A | THR99 |
A | THR100 |
A | ALA122 |
A | PRO123 |
A | ASN124 |
A | TYR125 |
A | ARG236 |
A | GLY11 |
A | ARG12 |
A | MET13 |
A | SER33 |
A | GLU34 |
A | ARG35 |
A | PHE75 |
A | THR76 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PG4 A 302 |
Chain | Residue |
A | GLY192 |
A | ILE193 |
C | GLY101 |
C | ALA162 |
C | PRO163 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue NAD B 301 |
Chain | Residue |
B | GLY8 |
B | GLY11 |
B | ARG12 |
B | MET13 |
B | SER33 |
B | GLU34 |
B | ARG35 |
B | PHE75 |
B | THR76 |
B | SER80 |
B | GLY98 |
B | THR100 |
B | ALA122 |
B | PRO123 |
B | ASN124 |
B | TYR125 |
B | LYS159 |
B | PHE239 |
B | 7FN302 |
B | HOH401 |
B | HOH419 |
B | HOH422 |
B | HOH425 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue 7FN B 302 |
Chain | Residue |
B | THR100 |
B | PRO123 |
B | HIS156 |
B | LYS159 |
B | SER164 |
B | GLY165 |
B | THR166 |
B | NAD301 |
B | HOH401 |
B | HOH403 |
B | HOH425 |
B | HOH428 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA B 303 |
Chain | Residue |
A | GLN109 |
A | HOH451 |
B | ALA21 |
B | HIS22 |
B | ASN24 |
B | ALA27 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PGE B 304 |
Chain | Residue |
B | GLY101 |
B | ALA162 |
B | ILE168 |
D | GLU191 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue NAD C 301 |
Chain | Residue |
C | GLY8 |
C | GLY11 |
C | ARG12 |
C | MET13 |
C | SER33 |
C | GLU34 |
C | ARG35 |
C | PHE75 |
C | THR76 |
C | SER80 |
C | GLY98 |
C | THR100 |
C | ALA122 |
C | PRO123 |
C | ASN124 |
C | TYR125 |
C | LYS159 |
C | 7FN302 |
C | HOH401 |
C | HOH402 |
C | HOH408 |
C | HOH410 |
C | HOH416 |
C | HOH422 |
C | HOH436 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue 7FN C 302 |
Chain | Residue |
C | GLY165 |
C | THR166 |
C | NAD301 |
C | HOH402 |
C | HOH405 |
C | HOH410 |
C | THR100 |
C | PRO123 |
C | HIS155 |
C | HIS156 |
C | LYS159 |
C | SER164 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue NA C 303 |
Chain | Residue |
C | ALA21 |
C | HIS22 |
C | ASN24 |
C | ALA27 |
D | GLN109 |
D | HOH470 |
site_id | AD1 |
Number of Residues | 25 |
Details | binding site for residue NAD D 301 |
Chain | Residue |
D | GLY8 |
D | GLY11 |
D | ARG12 |
D | MET13 |
D | SER33 |
D | GLU34 |
D | ARG35 |
D | PHE75 |
D | THR76 |
D | SER80 |
D | GLY98 |
D | THR100 |
D | ALA122 |
D | PRO123 |
D | ASN124 |
D | TYR125 |
D | LYS159 |
D | PHE239 |
D | 7FN302 |
D | HOH402 |
D | HOH420 |
D | HOH422 |
D | HOH440 |
D | HOH443 |
D | HOH448 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residue 7FN D 302 |
Chain | Residue |
D | THR100 |
D | PRO123 |
D | HIS156 |
D | LYS159 |
D | SER164 |
D | GLY165 |
D | THR166 |
D | NAD301 |
D | HOH402 |
D | HOH411 |
D | HOH414 |
D | HOH422 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue NA D 303 |
Chain | Residue |
D | ALA21 |
D | HIS22 |
D | ASN24 |
D | ALA27 |
D | HOH472 |
D | HOH474 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue NA D 304 |
Chain | Residue |
D | GLY179 |
D | ASN180 |
D | HOH444 |
D | HOH449 |
D | HOH457 |
Functional Information from PROSITE/UniProt
site_id | PS01298 |
Number of Residues | 18 |
Details | DAPB Dihydrodipicolinate reductase signature. EIvEaHhrhKvDapSGTA |
Chain | Residue | Details |
A | GLU150-ALA167 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | HIS155 | |
B | HIS155 | |
C | HIS155 | |
D | HIS155 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | LYS159 | |
B | LYS159 | |
C | LYS159 | |
D | LYS159 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | GLY8 | |
B | ARG35 | |
B | GLY98 | |
B | ALA122 | |
B | HIS156 | |
B | GLY165 | |
C | GLY8 | |
C | GLU34 | |
C | ARG35 | |
C | GLY98 | |
C | ALA122 | |
A | GLU34 | |
C | HIS156 | |
C | GLY165 | |
D | GLY8 | |
D | GLU34 | |
D | ARG35 | |
D | GLY98 | |
D | ALA122 | |
D | HIS156 | |
D | GLY165 | |
A | ARG35 | |
A | GLY98 | |
A | ALA122 | |
A | HIS156 | |
A | GLY165 | |
B | GLY8 | |
B | GLU34 |