2ESG
Solution structure of the complex between immunoglobulin IgA1 and human serum albumin
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005788 | cellular_component | endoplasmic reticulum lumen |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0008289 | molecular_function | lipid binding |
C | 0009267 | biological_process | cellular response to starvation |
C | 0015643 | molecular_function | toxic substance binding |
C | 0016209 | molecular_function | antioxidant activity |
C | 0019825 | molecular_function | oxygen 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 | 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 | 0140272 | molecular_function | exogenous protein binding |
C | 1903981 | molecular_function | enterobactin binding |
Functional Information from PROSITE/UniProt
site_id | PS00212 |
Number of Residues | 25 |
Details | ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL |
Chain | Residue | Details |
C | TYR161-LEU185 | |
C | TYR353-PHE377 | |
C | PHE551-LEU575 |
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FSCMVGH |
Chain | Residue | Details |
A | PHE433-HIS439 | |
L | TYR192-HIS198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:4373463 |
Chain | Residue | Details |
A | SER227 | |
A | SER241 | |
A | SER243 | |
B | SER227 | |
B | SER241 | |
B | SER243 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:20823119, ECO:0000269|PubMed:31959827 |
Chain | Residue | Details |
A | THR228 | |
A | THR231 | |
A | THR239 | |
B | THR228 | |
B | THR231 | |
B | THR239 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:20823119, ECO:0000269|PubMed:31959827, ECO:0000269|PubMed:4373463 |
Chain | Residue | Details |
A | SER233 | |
A | SER235 | |
B | SER233 | |
B | SER235 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:31959827 |
Chain | Residue | Details |
A | THR236 | |
B | THR236 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 |
Chain | Residue | Details |
A | ASN266 | |
C | LYS174 | |
C | LYS181 | |
C | LYS190 | |
C | LYS195 | |
C | LYS205 | |
C | LYS212 | |
C | LYS240 | |
C | LYS262 | |
C | LYS274 | |
C | LYS286 | |
B | ASN266 | |
C | LYS359 | |
C | LYS372 | |
C | LYS389 | |
C | LYS402 | |
C | LYS414 | |
C | LYS432 | |
C | LYS436 | |
C | LYS466 | |
C | LYS475 | |
C | LYS500 | |
C | LYS41 | |
C | LYS519 | |
C | LYS524 | |
C | LYS538 | |
C | LYS541 | |
C | LYS557 | |
C | LYS560 | |
C | LYS564 | |
C | LYS574 | |
C | LYS64 | |
C | LYS73 | |
C | LYS93 | |
C | LYS106 | |
C | LYS136 | |
C | LYS159 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Aspirin-acetylated lysine |
Chain | Residue | Details |
C | LYS199 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
C | SER5 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
C | SER58 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
C | SER65 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
C | THR83 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724 |
Chain | Residue | Details |
C | LYS205 | |
C | LYS436 | |
C | LYS519 | |
C | LYS564 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724 |
Chain | Residue | Details |
C | SER273 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
C | SER419 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
C | THR420 | |
C | THR422 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
C | SER489 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
C | LYS534 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 |
Chain | Residue | Details |
C | LYS12 | |
C | LYS281 | |
C | LYS317 | |
C | LYS439 |
site_id | SWS_FT_FI18 |
Number of Residues | 13 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 |
Chain | Residue | Details |
C | LYS51 | |
C | LYS444 | |
C | LYS536 | |
C | LYS545 | |
C | LYS573 | |
C | LYS137 | |
C | LYS162 | |
C | LYS225 | |
C | LYS276 | |
C | LYS313 | |
C | LYS323 | |
C | LYS378 | |
C | LYS413 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480 |
Chain | Residue | Details |
C | LYS199 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977 |
Chain | Residue | Details |
C | LYS233 | |
C | LYS351 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill |
Chain | Residue | Details |
C | ASN318 |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook |
Chain | Residue | Details |
C | ASP494 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480 |
Chain | Residue | Details |
C | LYS525 |
site_id | SWS_FT_FI24 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977 |
Chain | Residue | Details |
C | LYS534 |