Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0009536 | cellular_component | plastid |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase 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 | 0005794 | cellular_component | Golgi apparatus |
| B | 0005829 | cellular_component | cytosol |
| B | 0009536 | cellular_component | plastid |
| B | 0010494 | cellular_component | cytoplasmic stress granule |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016854 | molecular_function | racemase and epimerase 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 | 28 |
| Details | BINDING SITE FOR RESIDUE GDC A1376 |
| Chain | Residue |
| A | MET102 |
| A | HIS202 |
| A | ASN203 |
| A | GLU216 |
| A | LYS217 |
| A | ALA218 |
| A | ALA221 |
| A | PHE222 |
| A | LYS225 |
| A | TRP236 |
| A | GLN241 |
| A | GLY103 |
| A | ARG243 |
| A | MET277 |
| A | PRO300 |
| A | GLU301 |
| A | ARG306 |
| A | SER356 |
| A | HOH2438 |
| A | HOH2439 |
| A | HOH2440 |
| A | GLY104 |
| A | MET105 |
| A | ILE108 |
| A | SER143 |
| A | CYS145 |
| A | PHE174 |
| A | PHE201 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A1378 |
| Chain | Residue |
| A | GLY36 |
| A | GLY37 |
| A | PHE38 |
| A | ILE39 |
| A | ASP58 |
| A | TRP59 |
| 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 | PHE174 |
| A | LYS178 |
| A | PHE201 |
| A | ASN203 |
| A | ILE204 |
| A | LYS217 |
| A | HOH2072 |
| A | HOH2245 |
| A | HOH2441 |
| A | HOH2442 |
| A | HOH2443 |
| A | HOH2444 |
| A | HOH2445 |
| A | HOH2446 |
| A | HOH2447 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE GDC B1372 |
| Chain | Residue |
| B | MET102 |
| B | GLY103 |
| B | GLY104 |
| B | MET105 |
| B | ILE108 |
| B | SER143 |
| B | CYS145 |
| B | PHE174 |
| B | PHE201 |
| B | HIS202 |
| B | ASN203 |
| B | GLU216 |
| B | LYS217 |
| B | ALA218 |
| B | ALA221 |
| B | PHE222 |
| B | LYS225 |
| B | TRP236 |
| B | GLN241 |
| B | ARG243 |
| B | MET277 |
| B | PRO300 |
| B | GLU301 |
| B | ARG306 |
| B | SER356 |
| B | HOH2533 |
| B | HOH2534 |
| B | HOH2535 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD B1374 |
| Chain | Residue |
| B | LEU79 |
| B | ARG80 |
| B | LEU98 |
| B | ALA99 |
| B | ALA100 |
| B | MET102 |
| B | ILE122 |
| B | ALA141 |
| B | SER142 |
| B | SER143 |
| B | PHE174 |
| B | LYS178 |
| B | PHE201 |
| B | ASN203 |
| B | ILE204 |
| B | LYS217 |
| B | ARG371 |
| B | HOH2183 |
| B | HOH2330 |
| B | HOH2536 |
| B | HOH2537 |
| B | HOH2538 |
| B | HOH2539 |
| B | HOH2540 |
| B | HOH2541 |
| B | HOH2542 |
| B | GLY34 |
| B | GLY36 |
| B | GLY37 |
| B | PHE38 |
| B | ILE39 |
| B | ASP58 |
| B | TRP59 |
| B | LYS60 |
| B | VAL77 |
| B | ASP78 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BTB B1380 |
| Chain | Residue |
| A | GLU169 |
| A | PRO170 |
| A | GLN171 |
| A | HOH2179 |
| A | HOH2209 |
| B | TRP166 |
| B | GLU183 |
| B | LYS186 |
| B | HOH2553 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A1379 |
| Chain | Residue |
| A | TYR14 |
| A | LYS15 |
| A | GLU16 |
| B | ARG330 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A1380 |
| Chain | Residue |
| A | VAL77 |
| A | ASP78 |
| A | ASN84 |
| A | GLY368 |
| A | HOH2448 |
| A | HOH2450 |
| B | HIS295 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A1381 |
| Chain | Residue |
| A | GLY360 |
| A | THR361 |
| A | HOH2451 |
| A | HOH2452 |
| A | HOH2453 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A1382 |
| Chain | Residue |
| A | ARG19 |
| A | ARG46 |
| A | ASP249 |
| A | HOH2280 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A1383 |
| Chain | Residue |
| A | THR210 |
| A | TRP211 |
| A | LYS212 |
| A | HOH2454 |
| A | HOH2455 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A1384 |
| Chain | Residue |
| A | GLU162 |
| A | SER163 |
| A | HOH2200 |
| A | HOH2456 |
| A | HOH2457 |
| A | HOH2458 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A1385 |
| Chain | Residue |
| A | ASN189 |
| A | ARG264 |
| A | HOH2459 |
| A | HOH2460 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A1386 |
| Chain | Residue |
| A | ASN157 |
| A | HOH2194 |
| A | HOH2461 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A1387 |
| Chain | Residue |
| A | ARG257 |
| A | GLY318 |
| A | TRP319 |
| A | HOH2462 |
| A | HOH2463 |
| B | LYS29 |
| B | HOH2047 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A1388 |
| Chain | Residue |
| A | ASP101 |
| A | VAL114 |
| A | ARG215 |
| A | GLN362 |
| A | ARG371 |
| A | HOH2418 |
| A | HOH2464 |
| A | HOH2465 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A1389 |
| Chain | Residue |
| A | ASN62 |
| A | GLU63 |
| A | MET65 |
| A | GLY375 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A1390 |
| Chain | Residue |
| A | GLY213 |
| A | ARG224 |
| A | LEU352 |
| A | TYR353 |
| A | SER355 |
| A | LYS357 |
| A | HOH2260 |
| A | HOH2404 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B1375 |
| Chain | Residue |
| B | ASP272 |
| B | ASN307 |
| B | HOH2270 |
| B | HOH2438 |
| B | HOH2544 |
| B | HOH2545 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B1376 |
| Chain | Residue |
| B | ARG19 |
| B | ARG46 |
| B | ASP249 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B1377 |
| Chain | Residue |
| B | VAL77 |
| B | ASP78 |
| B | ASN84 |
| B | GLY368 |
| B | LEU370 |
| B | HOH2546 |
| B | HOH2547 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B1378 |
| Chain | Residue |
| B | GLU162 |
| B | SER163 |
| B | HOH2548 |
| B | HOH2549 |
| B | HOH2550 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT B1379 |
| Chain | Residue |
| B | LYS212 |
| B | GLY213 |
| B | ARG224 |
| B | LEU352 |
| B | TYR353 |
| B | SER355 |
| B | LYS357 |
| B | HOH2496 |
| B | HOH2552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16366586","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19376835","evidenceCode":"ECO:0007744"}]} |
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 | PHE174 | |
| A | LYS178 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER143 | |
| B | PHE174 | |
| B | LYS178 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER142 | |
| A | PHE174 | |
| A | LYS178 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER142 | |
| B | PHE174 | |
| B | LYS178 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER143 | |
| A | PHE174 | |
| 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 | PHE174 | |
| B | ASN119 | |
| B | LYS178 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | PHE174 | |
| A | LYS178 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | PHE174 | |
| B | LYS178 | |
