1MFZ
Partially refined 2.8 A Crystal structure of GDP-mannose dehydrogenase from P. aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006970 | biological_process | response to osmotic stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0036460 | biological_process | cellular response to cell envelope stress |
| A | 0042121 | biological_process | alginic acid biosynthetic process |
| A | 0044010 | biological_process | single-species biofilm formation |
| A | 0047919 | molecular_function | GDP-mannose 6-dehydrogenase activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0006970 | biological_process | response to osmotic stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0036460 | biological_process | cellular response to cell envelope stress |
| B | 0042121 | biological_process | alginic acid biosynthetic process |
| B | 0044010 | biological_process | single-species biofilm formation |
| B | 0047919 | molecular_function | GDP-mannose 6-dehydrogenase activity |
| B | 0051287 | molecular_function | NAD binding |
| C | 0006970 | biological_process | response to osmotic stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0036460 | biological_process | cellular response to cell envelope stress |
| C | 0042121 | biological_process | alginic acid biosynthetic process |
| C | 0044010 | biological_process | single-species biofilm formation |
| C | 0047919 | molecular_function | GDP-mannose 6-dehydrogenase activity |
| C | 0051287 | molecular_function | NAD binding |
| D | 0006970 | biological_process | response to osmotic stress |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0036460 | biological_process | cellular response to cell envelope stress |
| D | 0042121 | biological_process | alginic acid biosynthetic process |
| D | 0044010 | biological_process | single-species biofilm formation |
| D | 0047919 | molecular_function | GDP-mannose 6-dehydrogenase activity |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDX D 501 |
| Chain | Residue |
| C | GLU157 |
| C | ASN225 |
| D | TYR256 |
| D | TYR257 |
| D | MSE258 |
| D | ARG259 |
| D | PHE262 |
| D | PHE264 |
| D | GLY265 |
| D | CYS268 |
| D | LEU269 |
| C | PHE158 |
| D | PHE323 |
| D | LYS324 |
| D | HOH510 |
| C | LEU159 |
| C | ARG160 |
| C | GLU161 |
| C | LYS210 |
| C | ASN214 |
| C | HIS217 |
| C | VAL221 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE GDX D 502 |
| Chain | Residue |
| C | TYR256 |
| C | TYR257 |
| C | MSE258 |
| C | ARG259 |
| C | GLY261 |
| C | PHE262 |
| C | PHE264 |
| C | GLY265 |
| C | CYS268 |
| C | PHE323 |
| C | LYS324 |
| D | TYR10 |
| D | GLU157 |
| D | PHE158 |
| D | LEU159 |
| D | ARG160 |
| D | GLU161 |
| D | LYS210 |
| D | ASN214 |
| D | HIS217 |
| D | VAL221 |
| D | ASN225 |
| D | HOH519 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDX B 503 |
| Chain | Residue |
| A | GLU157 |
| A | PHE158 |
| A | LEU159 |
| A | ARG160 |
| A | GLU161 |
| A | LYS210 |
| A | ASN214 |
| A | HIS217 |
| A | VAL221 |
| A | ASN225 |
| B | LEU251 |
| B | TYR256 |
| B | TYR257 |
| B | MSE258 |
| B | ARG259 |
| B | PHE262 |
| B | PHE264 |
| B | GLY265 |
| B | CYS268 |
| B | LEU269 |
| B | PHE323 |
| B | LYS324 |
| B | HOH506 |
| B | HOH507 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDX B 504 |
| Chain | Residue |
| A | TYR256 |
| A | TYR257 |
| A | MSE258 |
| A | ARG259 |
| A | GLY261 |
| A | PHE262 |
| A | PHE264 |
| A | GLY265 |
| A | CYS268 |
| A | LEU269 |
| A | PHE323 |
| A | LYS324 |
| B | GLU157 |
| B | PHE158 |
| B | LEU159 |
| B | ARG160 |
| B | GLU161 |
| B | LYS210 |
| B | ASN214 |
| B | HIS217 |
| B | VAL221 |
| B | ASN225 |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVWH |
| Chain | Residue | Details |
| A | TYR211-HIS217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12705829 |
| Chain | Residue | Details |
| A | CYS268 | |
| B | CYS268 | |
| C | CYS268 | |
| D | CYS268 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: in chain A => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8 |
| Chain | Residue | Details |
| A | TYR10 | |
| B | LYS35 | |
| B | THR86 | |
| B | THR124 | |
| C | TYR10 | |
| C | VAL11 | |
| C | ASP30 | |
| C | LYS35 | |
| C | THR86 | |
| C | THR124 | |
| D | TYR10 | |
| A | VAL11 | |
| D | VAL11 | |
| D | ASP30 | |
| D | LYS35 | |
| D | THR86 | |
| D | THR124 | |
| A | ASP30 | |
| A | LYS35 | |
| A | THR86 | |
| A | THR124 | |
| B | TYR10 | |
| B | VAL11 | |
| B | ASP30 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: in chain A => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU |
| Chain | Residue | Details |
| A | GLU161 | |
| B | ASN225 | |
| C | GLU161 | |
| C | LYS210 | |
| C | ASN214 | |
| C | HIS217 | |
| C | ASN225 | |
| D | GLU161 | |
| D | LYS210 | |
| D | ASN214 | |
| D | HIS217 | |
| A | LYS210 | |
| D | ASN225 | |
| A | ASN214 | |
| A | HIS217 | |
| A | ASN225 | |
| B | GLU161 | |
| B | LYS210 | |
| B | ASN214 | |
| B | HIS217 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | BINDING: in chain B => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU |
| Chain | Residue | Details |
| A | TYR256 | |
| B | PHE262 | |
| B | GLY265 | |
| B | LYS324 | |
| C | TYR256 | |
| C | TYR257 | |
| C | ARG259 | |
| C | PHE262 | |
| C | GLY265 | |
| C | LYS324 | |
| D | TYR256 | |
| A | TYR257 | |
| D | TYR257 | |
| D | ARG259 | |
| D | PHE262 | |
| D | GLY265 | |
| D | LYS324 | |
| A | ARG259 | |
| A | PHE262 | |
| A | GLY265 | |
| A | LYS324 | |
| B | TYR256 | |
| B | TYR257 | |
| B | ARG259 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: in chain B => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8 |
| Chain | Residue | Details |
| A | LYS271 | |
| A | ARG331 | |
| B | LYS271 | |
| B | ARG331 | |
| C | LYS271 | |
| C | ARG331 | |
| D | LYS271 | |
| D | ARG331 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| A | ASP272 | |
| A | CYS268 | |
| A | GLU161 | |
| A | THR124 | |
| A | ASN214 | |
| A | LYS210 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| B | ASP272 | |
| B | CYS268 | |
| B | GLU161 | |
| B | THR124 | |
| B | ASN214 | |
| B | LYS210 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| C | ASP272 | |
| C | CYS268 | |
| C | GLU161 | |
| C | THR124 | |
| C | ASN214 | |
| C | LYS210 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dli |
| Chain | Residue | Details |
| D | ASP272 | |
| D | CYS268 | |
| D | GLU161 | |
| D | THR124 | |
| D | ASN214 | |
| D | LYS210 |
