Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005829 | cellular_component | cytosol |
A | 0009536 | cellular_component | plastid |
A | 0016853 | molecular_function | isomerase activity |
A | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
A | 0047918 | molecular_function | GDP-mannose 3,5-epimerase activity |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005829 | cellular_component | cytosol |
B | 0009536 | cellular_component | plastid |
B | 0016853 | molecular_function | isomerase activity |
B | 0019853 | biological_process | L-ascorbic acid biosynthetic process |
B | 0047918 | molecular_function | GDP-mannose 3,5-epimerase activity |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE GDD A1377 |
Chain | Residue |
A | MET102 |
A | ASN203 |
A | GLU216 |
A | LYS217 |
A | ALA218 |
A | ALA221 |
A | PHE222 |
A | LYS225 |
A | TRP236 |
A | GLN241 |
A | ARG243 |
A | GLY103 |
A | MET277 |
A | PRO300 |
A | GLU301 |
A | ARG306 |
A | SER356 |
A | HOH2217 |
A | HOH2295 |
A | HOH2380 |
A | GLY104 |
A | MET105 |
A | ILE108 |
A | SER143 |
A | ALA144 |
A | CYS145 |
A | TYR174 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE GDC A1378 |
Chain | Residue |
A | MET102 |
A | GLY103 |
A | GLY104 |
A | MET105 |
A | ILE108 |
A | SER143 |
A | CYS145 |
A | TYR174 |
A | PHE201 |
A | HIS202 |
A | ASN203 |
A | GLU216 |
A | LYS217 |
A | ALA218 |
A | ALA221 |
A | PHE222 |
A | LYS225 |
A | TRP236 |
A | GLN241 |
A | ARG243 |
A | MET277 |
A | PRO300 |
A | GLU301 |
A | ARG306 |
A | SER356 |
A | NAD1379 |
A | HOH2217 |
A | HOH2295 |
A | HOH2380 |
site_id | AC3 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE NAD A1379 |
Chain | Residue |
A | GLY34 |
A | GLY36 |
A | GLY37 |
A | PHE38 |
A | ILE39 |
A | ASP58 |
A | TRP59 |
A | LYS60 |
A | VAL77 |
A | ASP78 |
A | LEU79 |
A | ARG80 |
A | LEU98 |
A | ALA99 |
A | ALA100 |
A | MET102 |
A | ILE122 |
A | ALA141 |
A | SER142 |
A | SER143 |
A | TYR174 |
A | LYS178 |
A | PHE201 |
A | ASN203 |
A | ILE204 |
A | LYS217 |
A | GDC1378 |
A | HOH2097 |
A | HOH2381 |
A | HOH2382 |
A | HOH2383 |
A | HOH2384 |
A | HOH2385 |
A | HOH2386 |
A | HOH2387 |
A | HOH2388 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BTB B1376 |
Chain | Residue |
B | GLU90 |
B | GLY91 |
B | HOH2141 |
B | HOH2448 |
A | FMT1382 |
A | HOH2319 |
B | LYS29 |
B | TYR53 |
B | ILE55 |
B | GLU73 |
B | LYS87 |
site_id | AC5 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE GDD B1377 |
Chain | Residue |
B | MET102 |
B | GLY103 |
B | GLY104 |
B | MET105 |
B | ILE108 |
B | SER143 |
B | CYS145 |
B | TYR174 |
B | PHE201 |
B | HIS202 |
B | ASN203 |
B | GLU216 |
B | LYS217 |
B | ALA218 |
B | ALA221 |
B | PHE222 |
B | LYS225 |
B | MET235 |
B | TRP236 |
B | GLN241 |
B | ARG243 |
B | MET277 |
B | PRO300 |
B | GLU301 |
B | SER356 |
B | HOH2449 |
B | HOH2450 |
B | HOH2451 |
site_id | AC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE GDC B1378 |
Chain | Residue |
B | MET102 |
B | GLY103 |
B | GLY104 |
B | MET105 |
B | ILE108 |
B | SER143 |
B | CYS145 |
B | TYR174 |
B | PHE201 |
B | ASN203 |
B | GLU216 |
B | LYS217 |
B | ALA218 |
B | ALA221 |
B | PHE222 |
B | LYS225 |
B | MET235 |
B | TRP236 |
B | GLN241 |
B | ARG243 |
B | MET277 |
B | PRO300 |
B | GLU301 |
B | ARG306 |
B | SER356 |
B | NAD1380 |
B | HOH2449 |
B | HOH2450 |
B | HOH2451 |
site_id | AC7 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE NAD B1380 |
Chain | Residue |
B | GLY34 |
B | GLY36 |
B | GLY37 |
B | PHE38 |
B | ILE39 |
B | ASP58 |
B | TRP59 |
B | LYS60 |
B | VAL77 |
B | ASP78 |
B | LEU79 |
B | ARG80 |
B | LEU98 |
B | ALA99 |
B | ALA100 |
B | MET102 |
B | ILE122 |
B | ALA141 |
B | SER142 |
B | SER143 |
B | TYR174 |
B | LYS178 |
B | PHE201 |
B | ASN203 |
B | ILE204 |
B | LYS217 |
B | ARG371 |
B | GDC1378 |
B | HOH2152 |
B | HOH2156 |
B | HOH2282 |
B | HOH2452 |
B | HOH2453 |
B | HOH2454 |
B | HOH2455 |
B | HOH2456 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FMT A1380 |
Chain | Residue |
A | LYS212 |
A | GLY213 |
A | ARG224 |
A | LEU352 |
A | TYR353 |
A | SER355 |
A | LYS357 |
A | HOH2218 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A1381 |
Chain | Residue |
A | PHE150 |
B | PRO167 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A1382 |
Chain | Residue |
A | GLU18 |
A | ARG257 |
A | GLY318 |
A | TRP319 |
B | LYS29 |
B | BTB1376 |
B | HOH2147 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT B1371 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B1372 |
Chain | Residue |
B | ARG215 |
B | GLN362 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B1373 |
Chain | Residue |
B | SER229 |
B | THR230 |
B | ASP231 |
B | ARG232 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT B1374 |
Chain | Residue |
A | VAL77 |
A | ASP78 |
A | ASN84 |
A | GLY368 |
A | SER369 |
B | HIS295 |
B | HOH2444 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B1375 |
Chain | Residue |
A | PRO167 |
B | PHE150 |
B | HOH2445 |
B | HOH2446 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR174 | |
B | TYR174 | |
Chain | Residue | Details |
A | GLY34 | |
B | LYS178 | |
A | ASP58 | |
A | ASP78 | |
A | TYR174 | |
A | LYS178 | |
B | GLY34 | |
B | ASP58 | |
B | ASP78 | |
B | TYR174 | |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY103 | |
B | SER143 | |
B | ASN203 | |
B | GLU216 | |
B | LYS225 | |
B | GLN241 | |
B | ARG306 | |
B | SER356 | |
A | SER143 | |
A | ASN203 | |
A | GLU216 | |
A | LYS225 | |
A | GLN241 | |
A | ARG306 | |
A | SER356 | |
B | GLY103 | |
Chain | Residue | Details |
A | GLY2 | |
B | GLY2 | |
Chain | Residue | Details |
A | SER369 | |
B | SER369 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER143 | |
A | TYR174 | |
A | LYS178 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER143 | |
B | TYR174 | |
B | LYS178 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER142 | |
A | TYR174 | |
A | LYS178 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER142 | |
B | TYR174 | |
B | LYS178 | |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER143 | |
A | TYR174 | |
A | ASN119 | |
A | LYS178 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER143 | |
B | TYR174 | |
B | ASN119 | |
B | LYS178 | |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR174 | |
A | LYS178 | |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR174 | |
B | LYS178 | |