2Z95
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 | 24 |
Details | BINDING SITE FOR RESIDUE NDP A 1001 |
Chain | Residue |
A | GLY10 |
A | ALA83 |
A | ALA84 |
A | SER86 |
A | SER126 |
A | THR127 |
A | TYR151 |
A | LYS155 |
A | LEU178 |
A | ASN180 |
A | HIS181 |
A | ARG12 |
A | ARG186 |
A | HOH1031 |
A | HOH1043 |
A | HOH1060 |
A | HOH1074 |
A | GLY13 |
A | GLN14 |
A | ASP15 |
A | ARG35 |
A | ASP60 |
A | LEU61 |
A | LEU82 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GDP D 1002 |
Chain | Residue |
D | GLU129 |
D | ASN180 |
D | GLU189 |
D | PHE190 |
D | LYS194 |
D | GLY213 |
D | ASN214 |
D | ALA217 |
D | ARG219 |
D | ARG297 |
D | GLU300 |
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 |