2Z1M
Crystal Structure of GDP-D-Mannose Dehydratase from Aquifex aeolicus VF5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019673 | biological_process | GDP-mannose metabolic process |
| A | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019673 | biological_process | GDP-mannose metabolic process |
| B | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
| B | 0070401 | molecular_function | NADP+ binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019673 | biological_process | GDP-mannose metabolic process |
| C | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
| C | 0070401 | molecular_function | NADP+ binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008446 | molecular_function | GDP-mannose 4,6-dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019673 | biological_process | GDP-mannose metabolic process |
| D | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
| D | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP A 1001 |
| Chain | Residue |
| A | GLY13 |
| A | LEU82 |
| A | ALA83 |
| A | ALA84 |
| A | SER86 |
| A | SER126 |
| A | THR127 |
| A | TYR151 |
| A | LYS155 |
| A | LEU178 |
| A | ASN180 |
| A | GLN14 |
| A | HIS181 |
| A | ARG186 |
| A | HOH1011 |
| A | HOH1030 |
| A | HOH1042 |
| A | HOH1067 |
| A | HOH1104 |
| A | HOH1111 |
| A | HOH1119 |
| A | ASP15 |
| A | ASP34 |
| A | ARG35 |
| A | ARG36 |
| A | MET59 |
| A | ASP60 |
| A | LEU61 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDP A 1002 |
| Chain | Residue |
| A | VAL88 |
| A | GLU129 |
| A | ASN180 |
| A | GLU189 |
| A | VAL191 |
| A | LYS194 |
| A | LEU212 |
| A | GLY213 |
| A | ASN214 |
| A | ALA217 |
| A | ARG219 |
| A | VAL253 |
| A | PHE295 |
| A | ARG297 |
| A | GLU300 |
| A | HOH1017 |
| A | HOH1032 |
| A | HOH1035 |
| A | HOH1083 |
| A | HOH1087 |
| A | HOH1095 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP D 1101 |
| Chain | Residue |
| D | GLY13 |
| D | GLN14 |
| D | ASP15 |
| D | ASP34 |
| D | ARG35 |
| D | ARG36 |
| D | MET59 |
| D | ASP60 |
| D | LEU61 |
| D | LEU82 |
| D | ALA83 |
| D | ALA84 |
| D | SER86 |
| D | ALA125 |
| D | SER126 |
| D | THR127 |
| D | TYR151 |
| D | LYS155 |
| D | LEU178 |
| D | ASN180 |
| D | HIS181 |
| D | ARG186 |
| D | HOH1119 |
| D | HOH1132 |
| D | HOH1138 |
| D | HOH1185 |
| D | HOH1200 |
| D | HOH1239 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP D 1102 |
| Chain | Residue |
| D | VAL88 |
| D | GLU129 |
| D | ASN180 |
| D | GLU189 |
| D | VAL191 |
| D | LYS194 |
| D | LEU212 |
| D | GLY213 |
| D | ASN214 |
| D | ALA217 |
| D | ARG219 |
| D | VAL253 |
| D | PHE295 |
| D | ARG297 |
| D | GLU300 |
| D | HOH1117 |
| D | HOH1123 |
| D | HOH1131 |
| D | HOH1184 |
| D | HOH1194 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. PqtektpfypRspYAVAKLFGhWITvNYR |
| Chain | Residue | Details |
| A | PRO138-ARG166 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | TYR151 | |
| A | THR127 | |
| A | GLU129 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | ARG148 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | LYS155 | |
| C | ARG148 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | LYS155 | |
| D | ARG148 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | TYR151 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | TYR151 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | LYS155 | |
| C | TYR151 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | LYS155 | |
| D | TYR151 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | TYR151 | |
| B | THR127 | |
| B | GLU129 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | LYS155 | |
| C | TYR151 | |
| C | THR127 | |
| C | GLU129 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | LYS155 | |
| D | TYR151 | |
| D | THR127 | |
| D | GLU129 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | TYR151 | |
| A | THR127 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS155 | |
| B | TYR151 | |
| B | THR127 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| C | LYS155 | |
| C | TYR151 | |
| C | THR127 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| D | LYS155 | |
| D | TYR151 | |
| D | THR127 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | ARG148 |
