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 |