5Z0B
Crystal structure of plasma-derived human serum albumin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009267 | biological_process | cellular response to starvation |
| A | 0015643 | molecular_function | toxic substance binding |
| A | 0015723 | biological_process | bilirubin transport |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0031667 | biological_process | response to nutrient levels |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042167 | biological_process | heme catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0072732 | biological_process | cellular response to calcium ion starvation |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140104 | molecular_function | molecular carrier activity |
| A | 0140272 | molecular_function | exogenous protein binding |
| A | 1903981 | molecular_function | enterobactin binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009267 | biological_process | cellular response to starvation |
| B | 0015643 | molecular_function | toxic substance binding |
| B | 0015723 | biological_process | bilirubin transport |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031093 | cellular_component | platelet alpha granule lumen |
| B | 0031667 | biological_process | response to nutrient levels |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042167 | biological_process | heme catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0072732 | biological_process | cellular response to calcium ion starvation |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0140104 | molecular_function | molecular carrier activity |
| B | 0140272 | molecular_function | exogenous protein binding |
| B | 1903981 | molecular_function | enterobactin binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005504 | molecular_function | fatty acid binding |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005788 | cellular_component | endoplasmic reticulum lumen |
| C | 0006783 | biological_process | heme biosynthetic process |
| C | 0008289 | molecular_function | lipid binding |
| C | 0009267 | biological_process | cellular response to starvation |
| C | 0015643 | molecular_function | toxic substance binding |
| C | 0015723 | biological_process | bilirubin transport |
| C | 0016209 | molecular_function | antioxidant activity |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0031093 | cellular_component | platelet alpha granule lumen |
| C | 0031667 | biological_process | response to nutrient levels |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0042167 | biological_process | heme catabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0072562 | cellular_component | blood microparticle |
| C | 0072732 | biological_process | cellular response to calcium ion starvation |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0140104 | molecular_function | molecular carrier activity |
| C | 0140272 | molecular_function | exogenous protein binding |
| C | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EIC A 601 |
| Chain | Residue |
| A | LYS195 |
| A | LYS199 |
| A | PHE211 |
| A | TRP214 |
| A | TYR452 |
| A | SO4607 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue OCA A 602 |
| Chain | Residue |
| A | LEU250 |
| A | LEU251 |
| A | VAL46 |
| A | PHE70 |
| A | GLY248 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PLM A 603 |
| Chain | Residue |
| A | TYR138 |
| A | ARG145 |
| A | HIS146 |
| A | TYR161 |
| A | LEU185 |
| A | ARG186 |
| A | GLY189 |
| A | LYS190 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue OCA A 604 |
| Chain | Residue |
| A | ALA213 |
| A | LEU327 |
| A | LYS351 |
| A | GLU354 |
| A | HOH1042 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue TRP A 605 |
| Chain | Residue |
| A | LEU387 |
| A | ASN391 |
| A | LEU407 |
| A | ARG410 |
| A | TYR411 |
| A | LEU430 |
| A | VAL433 |
| A | GLY434 |
| A | SER489 |
| A | HOH1100 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ARG186 |
| A | LYS190 |
| A | ARG428 |
| A | LYS432 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | TYR150 |
| A | LYS199 |
| A | LEU238 |
| A | HIS242 |
| A | ARG257 |
| A | ALA291 |
| A | EIC601 |
| A | HOH1044 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | GLN417 |
| A | SER470 |
| A | ASP471 |
| A | ARG472 |
| A | ASP494 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | SER419 |
| A | THR420 |
| A | LYS500 |
| A | LYS534 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 610 |
| Chain | Residue |
| A | GLU400 |
| A | TYR401 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 611 |
| Chain | Residue |
| A | LYS351 |
| A | SER480 |
| A | LEU481 |
| A | VAL482 |
| A | HOH1072 |
| A | HOH1091 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 612 |
| Chain | Residue |
| A | ASP121 |
| A | ALA172 |
| A | ASP173 |
| A | LYS174 |
| A | ALA175 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 613 |
| Chain | Residue |
| A | THR540 |
| A | LYS541 |
| B | LYS372 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 614 |
| Chain | Residue |
| A | TYR452 |
| A | HOH1085 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 615 |
| Chain | Residue |
| A | GLU277 |
| A | GLU280 |
| A | LYS281 |
| C | MET298 |
| C | HOH1086 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue PG4 A 616 |
| Chain | Residue |
| A | THR236 |
| A | THR243 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 617 |
| Chain | Residue |
| A | ARG348 |
| A | THR352 |
| A | ASN483 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 A 618 |
| Chain | Residue |
| A | LYS205 |
| A | LYS323 |
| A | GLU465 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 619 |
| Chain | Residue |
| A | LYS225 |
| A | ASP269 |
| A | SER270 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue EIC B 601 |
| Chain | Residue |
| B | LYS195 |
| B | LYS199 |
| B | PHE211 |
| B | TRP214 |
| B | ARG218 |
| B | TYR452 |
| B | SO4606 |
| B | HOH1040 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue OCA B 602 |
| Chain | Residue |
| B | PHE70 |
| B | LYS73 |
| B | GLY248 |
| B | LEU250 |
| B | LEU251 |
| B | VAL46 |
| B | LEU69 |
| site_id | AE4 |
| Number of Residues | 10 |
| Details | binding site for residue PLM B 603 |
| Chain | Residue |
| B | ARG114 |
| B | TYR138 |
| B | ILE142 |
| B | HIS146 |
| B | PHE149 |
| B | TYR161 |
| B | LEU185 |
| B | ARG186 |
| B | GLY189 |
| B | LYS190 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue PLM B 604 |
| Chain | Residue |
| B | ALA213 |
| B | VAL216 |
| B | LEU327 |
| B | LYS351 |
| B | GLU354 |
| B | HOH1084 |
| B | HOH1175 |
| C | HOH1123 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue TRP B 605 |
| Chain | Residue |
| B | LEU387 |
| B | ASN391 |
| B | ARG410 |
| B | TYR411 |
| B | LEU430 |
| B | VAL433 |
| B | GLY434 |
| B | SER489 |
| site_id | AE7 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | TYR150 |
| B | LYS199 |
| B | LEU238 |
| B | HIS242 |
| B | ARG257 |
| B | ALA291 |
| B | EIC601 |
| B | HOH1125 |
| B | HOH1136 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 607 |
| Chain | Residue |
| B | GLN417 |
| B | SER470 |
| B | ASP471 |
| B | ARG472 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 608 |
| Chain | Residue |
| B | SER419 |
| B | THR420 |
| B | LYS500 |
| B | LYS534 |
| site_id | AF1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 609 |
| Chain | Residue |
| B | GLU400 |
| B | TYR401 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 610 |
| Chain | Residue |
| B | ARG186 |
| B | LYS190 |
| B | ARG428 |
| B | LYS432 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 611 |
| Chain | Residue |
| B | LYS351 |
| B | SER480 |
| B | LEU481 |
| B | VAL482 |
| B | PEG616 |
| B | HOH1071 |
| site_id | AF4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 612 |
| Chain | Residue |
| A | LYS372 |
| B | THR540 |
| B | LYS541 |
| site_id | AF5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 613 |
| Chain | Residue |
| B | PHE134 |
| B | LYS137 |
| B | TYR161 |
| site_id | AF6 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 614 |
| Chain | Residue |
| B | TYR452 |
| B | VAL456 |
| site_id | AF7 |
| Number of Residues | 6 |
| Details | binding site for residue PGE B 615 |
| Chain | Residue |
| B | LYS233 |
| B | ASP237 |
| B | ASP256 |
| B | ASP259 |
| B | LEU260 |
| B | HOH1174 |
| site_id | AF8 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 616 |
| Chain | Residue |
| B | ARG348 |
| B | THR352 |
| B | ASN483 |
| B | SO4611 |
| site_id | AF9 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 617 |
| Chain | Residue |
| B | SER58 |
| B | ASP63 |
| B | PRO299 |
| B | HOH1053 |
| site_id | AG1 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 B 618 |
| Chain | Residue |
| A | GLU297 |
| B | LYS225 |
| B | ASP269 |
| B | SER272 |
| B | HOH1172 |
| site_id | AG2 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 619 |
| Chain | Residue |
| B | GLU354 |
| B | HOH1170 |
| site_id | AG3 |
| Number of Residues | 1 |
| Details | binding site for residue PEG B 620 |
| Chain | Residue |
| B | THR356 |
| site_id | AG4 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE B 622 |
| Chain | Residue |
| B | LYS323 |
| B | GLU358 |
| B | HOH1170 |
| C | LYS205 |
| C | PHE206 |
| C | THR478 |
| site_id | AG5 |
| Number of Residues | 2 |
| Details | binding site for residue PGE B 623 |
| Chain | Residue |
| B | THR243 |
| B | ASP249 |
| site_id | AG6 |
| Number of Residues | 8 |
| Details | binding site for residue EIC C 601 |
| Chain | Residue |
| C | LYS195 |
| C | LYS199 |
| C | PHE211 |
| C | TRP214 |
| C | ARG218 |
| C | ASP451 |
| C | VAL455 |
| C | SO4607 |
| site_id | AG7 |
| Number of Residues | 6 |
| Details | binding site for residue OCA C 602 |
| Chain | Residue |
| C | PHE70 |
| C | LYS73 |
| C | GLY248 |
| C | LEU250 |
| C | LEU251 |
| C | PEG613 |
| site_id | AG8 |
| Number of Residues | 7 |
| Details | binding site for residue PLM C 603 |
| Chain | Residue |
| C | TYR138 |
| C | HIS146 |
| C | PHE157 |
| C | TYR161 |
| C | LEU185 |
| C | GLY189 |
| C | LYS190 |
| site_id | AG9 |
| Number of Residues | 3 |
| Details | binding site for residue OCA C 604 |
| Chain | Residue |
| C | LYS351 |
| C | GLU354 |
| C | HOH1101 |
| site_id | AH1 |
| Number of Residues | 8 |
| Details | binding site for residue TRP C 605 |
| Chain | Residue |
| C | ASN391 |
| C | PHE403 |
| C | LEU407 |
| C | ARG410 |
| C | TYR411 |
| C | LEU430 |
| C | GLY434 |
| C | SER489 |
| site_id | AH2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 606 |
| Chain | Residue |
| C | LYS351 |
| C | SER480 |
| C | LEU481 |
| C | VAL482 |
| C | PEG610 |
| site_id | AH3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 C 607 |
| Chain | Residue |
| C | TYR150 |
| C | LYS199 |
| C | LEU238 |
| C | HIS242 |
| C | ARG257 |
| C | ALA291 |
| C | EIC601 |
| C | HOH1036 |
| C | HOH1094 |
| site_id | AH4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 608 |
| Chain | Residue |
| C | GLN417 |
| C | SER470 |
| C | ASP471 |
| C | ARG472 |
| C | THR496 |
| site_id | AH5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 609 |
| Chain | Residue |
| C | SER304 |
| C | LEU305 |
| C | ALA306 |
| C | ARG337 |
| site_id | AH6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG C 610 |
| Chain | Residue |
| C | ARG348 |
| C | SER480 |
| C | ASN483 |
| C | SO4606 |
| site_id | AH7 |
| Number of Residues | 3 |
| Details | binding site for residue PGE C 611 |
| Chain | Residue |
| C | LYS225 |
| C | ASP269 |
| C | HOH1141 |
| site_id | AH8 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 C 612 |
| Chain | Residue |
| B | LYS205 |
| B | GLU465 |
| C | ALA320 |
| C | LYS323 |
| site_id | AH9 |
| Number of Residues | 2 |
| Details | binding site for residue PEG C 613 |
| Chain | Residue |
| C | LYS73 |
| C | OCA602 |
| site_id | AI1 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 C 614 |
| Chain | Residue |
| B | HOH1175 |
| C | GLU244 |
| C | ASP249 |
| site_id | AI2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG C 615 |
| Chain | Residue |
| C | LYS190 |
| C | SER193 |
| C | ALA194 |
| C | GLN459 |
Functional Information from PROSITE/UniProt
| site_id | PS00212 |
| Number of Residues | 25 |
| Details | ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL |
| Chain | Residue | Details |
| A | TYR161-LEU185 | |
| A | TYR353-PHE377 | |
| A | PHE551-LEU575 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 576 |
| Details | Domain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 394 |
| Details | Domain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28567254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IJF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 107 |
| Details | Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Site: {"description":"Aspirin-acetylated lysine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 11 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 38 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6706980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
