7KF3
Crystal structure of GDP-mannose 4,6-dehydratase from Brucella abortus (strain 2308) in complex with Guanosine-diphosphate-rhamnose
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 GDR A 400 |
| Chain | Residue |
| A | SER90 |
| A | VAL197 |
| A | LYS200 |
| A | LEU218 |
| A | GLY219 |
| A | ASN220 |
| A | SER223 |
| A | ARG225 |
| A | VAL259 |
| A | ARG303 |
| A | GLU306 |
| A | VAL92 |
| A | VAL307 |
| A | NAP401 |
| A | HOH515 |
| A | HOH517 |
| A | HOH528 |
| A | HOH537 |
| A | HOH544 |
| A | HOH561 |
| A | HOH568 |
| A | THR133 |
| A | GLU135 |
| A | TYR157 |
| A | ASN186 |
| A | ARG192 |
| A | THR195 |
| A | PHE196 |
| site_id | AC2 |
| Number of Residues | 39 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | GLY9 |
| A | THR11 |
| A | GLY12 |
| A | GLN13 |
| A | ASP14 |
| A | ARG34 |
| A | ASN40 |
| A | ASP64 |
| A | LEU65 |
| A | LEU86 |
| A | GLY87 |
| A | ALA88 |
| A | SER90 |
| A | TYR101 |
| A | SER105 |
| A | ALA131 |
| A | SER132 |
| A | THR133 |
| A | TYR157 |
| A | LYS161 |
| A | LEU184 |
| A | ASN186 |
| A | HIS187 |
| A | ARG192 |
| A | GDR400 |
| A | HOH520 |
| A | HOH541 |
| A | HOH547 |
| A | HOH558 |
| A | HOH564 |
| A | HOH568 |
| A | HOH569 |
| A | HOH578 |
| A | HOH588 |
| A | HOH603 |
| A | HOH608 |
| B | THR36 |
| B | SER37 |
| B | HOH507 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue GDR B 400 |
| Chain | Residue |
| B | SER90 |
| B | VAL92 |
| B | THR133 |
| B | SER134 |
| B | GLU135 |
| B | TYR157 |
| B | ASN186 |
| B | ARG192 |
| B | THR195 |
| B | PHE196 |
| B | VAL197 |
| B | LYS200 |
| B | LEU218 |
| B | GLY219 |
| B | ASN220 |
| B | SER223 |
| B | ARG225 |
| B | VAL259 |
| B | TYR301 |
| B | ARG303 |
| B | GLU306 |
| B | VAL307 |
| B | NAP401 |
| B | HOH506 |
| B | HOH521 |
| B | HOH522 |
| B | HOH533 |
| B | HOH545 |
| B | HOH548 |
| site_id | AC4 |
| Number of Residues | 41 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| A | HOH508 |
| B | GLY9 |
| B | THR11 |
| B | GLY12 |
| B | GLN13 |
| B | ASP14 |
| B | ARG34 |
| B | ASN40 |
| B | ASP64 |
| B | LEU65 |
| B | LEU86 |
| B | GLY87 |
| B | ALA88 |
| B | SER90 |
| B | TYR101 |
| B | SER105 |
| B | ALA131 |
| B | SER132 |
| B | THR133 |
| B | TYR157 |
| B | LYS161 |
| B | LEU184 |
| B | ASN186 |
| B | HIS187 |
| B | ARG192 |
| B | GDR400 |
| B | HOH510 |
| B | HOH523 |
| B | HOH541 |
| B | HOH544 |
| B | HOH545 |
| B | HOH552 |
| B | HOH555 |
| B | HOH561 |
| B | HOH566 |
| B | HOH572 |
| B | HOH585 |
| B | HOH597 |
| A | ARG35 |
| A | THR36 |
| A | SER37 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | binding site for residue GDR C 400 |
| Chain | Residue |
| C | SER90 |
| C | VAL92 |
| C | THR133 |
| C | SER134 |
| C | GLU135 |
| C | TYR157 |
| C | ASN186 |
| C | ARG192 |
| C | THR195 |
| C | PHE196 |
| C | VAL197 |
| C | LYS200 |
| C | LEU218 |
| C | GLY219 |
| C | ASN220 |
| C | SER223 |
| C | ARG225 |
| C | VAL259 |
| C | ARG303 |
| C | GLU306 |
| C | VAL307 |
| C | NAP401 |
| C | HOH520 |
| C | HOH527 |
| C | HOH535 |
| C | HOH542 |
| C | HOH546 |
| C | HOH581 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | binding site for residue NAP C 401 |
| Chain | Residue |
| C | GLY9 |
| C | THR11 |
| C | GLY12 |
| C | GLN13 |
| C | ASP14 |
| C | ARG34 |
| C | ASN40 |
| C | ASP64 |
| C | LEU65 |
| C | LEU86 |
| C | GLY87 |
| C | ALA88 |
| C | SER90 |
| C | TYR101 |
| C | SER105 |
| C | ALA131 |
| C | SER132 |
| C | THR133 |
| C | TYR157 |
| C | LYS161 |
| C | LEU184 |
| C | ASN186 |
| C | HIS187 |
| C | ARG192 |
| C | GDR400 |
| C | HOH519 |
| C | HOH522 |
| C | HOH530 |
| C | HOH540 |
| C | HOH542 |
| C | HOH547 |
| C | HOH558 |
| C | HOH566 |
| C | HOH576 |
| C | HOH586 |
| D | ARG35 |
| D | THR36 |
| D | SER37 |
| D | HOH533 |
| D | HOH577 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue GDR D 400 |
| Chain | Residue |
| D | SER90 |
| D | VAL92 |
| D | THR133 |
| D | SER134 |
| D | GLU135 |
| D | TYR157 |
| D | ASN186 |
| D | ARG192 |
| D | THR195 |
| D | PHE196 |
| D | VAL197 |
| D | LYS200 |
| D | LEU218 |
| D | GLY219 |
| D | ASN220 |
| D | SER223 |
| D | ARG225 |
| D | VAL259 |
| D | TYR301 |
| D | ARG303 |
| D | GLU306 |
| D | VAL307 |
| D | NAP401 |
| D | HOH509 |
| D | HOH514 |
| D | HOH516 |
| D | HOH517 |
| D | HOH537 |
| D | HOH542 |
| D | HOH555 |
| site_id | AC8 |
| Number of Residues | 41 |
| Details | binding site for residue NAP D 401 |
| Chain | Residue |
| C | ARG35 |
| C | THR36 |
| C | SER37 |
| C | HOH518 |
| C | HOH531 |
| D | GLY9 |
| D | THR11 |
| D | GLY12 |
| D | GLN13 |
| D | ASP14 |
| D | ARG34 |
| D | ASN40 |
| D | ASP64 |
| D | LEU65 |
| D | LEU86 |
| D | GLY87 |
| D | ALA88 |
| D | SER90 |
| D | TYR101 |
| D | SER105 |
| D | ALA131 |
| D | SER132 |
| D | THR133 |
| D | TYR157 |
| D | LYS161 |
| D | LEU184 |
| D | ASN186 |
| D | HIS187 |
| D | ARG192 |
| D | GDR400 |
| D | HOH513 |
| D | HOH521 |
| D | HOH529 |
| D | HOH534 |
| D | HOH541 |
| D | HOH551 |
| D | HOH555 |
| D | HOH566 |
| D | HOH575 |
| D | HOH578 |
| D | HOH579 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. PqkettpfypRspYAAAKLYAyWITvNYR |
| Chain | Residue | Details |
| A | PRO144-ARG172 |
