4Z69
Human serum albumin complexed with palmitic acid and diclofenac
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 | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009267 | biological_process | cellular response to starvation |
| A | 0015643 | molecular_function | toxic substance binding |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0032991 | cellular_component | protein-containing complex |
| 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 | 0140272 | molecular_function | exogenous protein binding |
| A | 1903981 | molecular_function | enterobactin binding |
| I | 0003677 | molecular_function | DNA binding |
| I | 0005504 | molecular_function | fatty acid binding |
| I | 0005507 | molecular_function | copper ion binding |
| I | 0005515 | molecular_function | protein binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005615 | cellular_component | extracellular space |
| I | 0005634 | cellular_component | nucleus |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005783 | cellular_component | endoplasmic reticulum |
| I | 0005788 | cellular_component | endoplasmic reticulum lumen |
| I | 0005794 | cellular_component | Golgi apparatus |
| I | 0008289 | molecular_function | lipid binding |
| I | 0009267 | biological_process | cellular response to starvation |
| I | 0015643 | molecular_function | toxic substance binding |
| I | 0016209 | molecular_function | antioxidant activity |
| I | 0019825 | molecular_function | oxygen binding |
| I | 0030170 | molecular_function | pyridoxal phosphate binding |
| I | 0031093 | cellular_component | platelet alpha granule lumen |
| I | 0032991 | cellular_component | protein-containing complex |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051087 | molecular_function | protein-folding chaperone binding |
| I | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| I | 0070062 | cellular_component | extracellular exosome |
| I | 0072562 | cellular_component | blood microparticle |
| I | 0072732 | biological_process | cellular response to calcium ion starvation |
| I | 0098869 | biological_process | cellular oxidant detoxification |
| I | 0140272 | molecular_function | exogenous protein binding |
| I | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue F15 A 1001 |
| Chain | Residue |
| A | ARG117 |
| A | TYR138 |
| A | TYR161 |
| A | DIF1006 |
| A | HOH1131 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue PLM A 1002 |
| Chain | Residue |
| A | ALA258 |
| A | SER287 |
| A | HOH1148 |
| A | LEU66 |
| A | PHE70 |
| A | TYR150 |
| A | ARG257 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue F15 A 1003 |
| Chain | Residue |
| A | SER342 |
| A | VAL344 |
| A | ARG348 |
| A | LEU387 |
| A | LEU453 |
| A | ARG485 |
| A | PLM1004 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PLM A 1004 |
| Chain | Residue |
| A | TYR411 |
| A | LEU460 |
| A | PHE488 |
| A | SER489 |
| A | F151003 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue F15 A 1005 |
| Chain | Residue |
| A | TYR401 |
| A | LYS525 |
| A | HIS535 |
| A | MET548 |
| A | PHE551 |
| A | ALA552 |
| A | SER579 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue DIF A 1006 |
| Chain | Residue |
| A | ILE142 |
| A | HIS146 |
| A | PHE149 |
| A | LEU154 |
| A | TYR161 |
| A | ARG186 |
| A | GLY189 |
| A | LYS190 |
| A | F151001 |
| A | HOH1175 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue DIF A 1007 |
| Chain | Residue |
| A | LYS199 |
| A | TRP214 |
| A | ARG218 |
| A | LEU219 |
| A | ARG222 |
| A | ILE264 |
| A | SER287 |
| A | HOH1146 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue DIF A 1008 |
| Chain | Residue |
| A | LYS199 |
| A | SER202 |
| A | LEU203 |
| A | PHE206 |
| A | ALA210 |
| A | PHE211 |
| A | TRP214 |
| A | VAL344 |
| A | SER480 |
| A | LEU481 |
| A | VAL482 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue F15 I 1001 |
| Chain | Residue |
| I | TYR138 |
| I | TYR161 |
| I | HOH1150 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue PLM I 1002 |
| Chain | Residue |
| I | VAL46 |
| I | PHE70 |
| I | TYR150 |
| I | ALA254 |
| I | ARG257 |
| I | LEU283 |
| I | LEU284 |
| I | SER287 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue F15 I 1003 |
| Chain | Residue |
| I | SER342 |
| I | VAL344 |
| I | ARG348 |
| I | LEU387 |
| I | LEU453 |
| I | ARG485 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PLM I 1004 |
| Chain | Residue |
| I | LEU387 |
| I | TYR411 |
| I | LEU457 |
| I | LEU460 |
| I | PHE488 |
| I | SER489 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue F15 I 1005 |
| Chain | Residue |
| I | TYR401 |
| I | LYS525 |
| I | HIS535 |
| I | PHE551 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue DIF I 1006 |
| Chain | Residue |
| I | LYS199 |
| I | TRP214 |
| I | ARG218 |
| I | ARG222 |
| I | PHE223 |
| I | ARG257 |
| I | LEU260 |
| I | ALA291 |
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 | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02770 |
| Chain | Residue | Details |
| A | HIS3 | |
| I | HIS3 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02769 |
| Chain | Residue | Details |
| A | GLU6 | |
| I | GLU252 | |
| I | ASP255 | |
| I | ASP259 | |
| A | ASP13 | |
| A | GLU244 | |
| A | GLU252 | |
| A | ASP255 | |
| A | ASP259 | |
| I | GLU6 | |
| I | ASP13 | |
| I | GLU244 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF |
| Chain | Residue | Details |
| A | HIS67 | |
| A | HIS247 | |
| A | ASP249 | |
| I | HIS67 | |
| I | HIS247 | |
| I | ASP249 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:656055 |
| Chain | Residue | Details |
| A | LYS240 | |
| I | LYS240 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 74 |
| Details | SITE: Not glycated => ECO:0000269|PubMed:15047055 |
| Chain | Residue | Details |
| A | LYS4 | |
| A | LYS174 | |
| A | LYS181 | |
| A | LYS190 | |
| A | LYS195 | |
| A | LYS205 | |
| A | LYS212 | |
| A | LYS240 | |
| A | LYS262 | |
| A | LYS274 | |
| A | LYS286 | |
| A | LYS20 | |
| A | LYS359 | |
| A | LYS372 | |
| A | LYS389 | |
| A | LYS402 | |
| A | LYS414 | |
| A | LYS432 | |
| A | LYS436 | |
| A | LYS466 | |
| A | LYS475 | |
| A | LYS500 | |
| A | LYS41 | |
| A | LYS519 | |
| A | LYS524 | |
| A | LYS538 | |
| A | LYS541 | |
| A | LYS557 | |
| A | LYS560 | |
| A | LYS564 | |
| A | LYS574 | |
| I | LYS4 | |
| I | LYS20 | |
| A | LYS64 | |
| I | LYS41 | |
| I | LYS64 | |
| I | LYS73 | |
| I | LYS93 | |
| I | LYS106 | |
| I | LYS136 | |
| I | LYS159 | |
| I | LYS174 | |
| I | LYS181 | |
| I | LYS190 | |
| A | LYS73 | |
| I | LYS195 | |
| I | LYS205 | |
| I | LYS212 | |
| I | LYS240 | |
| I | LYS262 | |
| I | LYS274 | |
| I | LYS286 | |
| I | LYS359 | |
| I | LYS372 | |
| I | LYS389 | |
| A | LYS93 | |
| I | LYS402 | |
| I | LYS414 | |
| I | LYS432 | |
| I | LYS436 | |
| I | LYS466 | |
| I | LYS475 | |
| I | LYS500 | |
| I | LYS519 | |
| I | LYS524 | |
| I | LYS538 | |
| A | LYS106 | |
| I | LYS541 | |
| I | LYS557 | |
| I | LYS560 | |
| I | LYS564 | |
| I | LYS574 | |
| A | LYS136 | |
| A | LYS159 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Aspirin-acetylated lysine |
| Chain | Residue | Details |
| A | LYS199 | |
| I | LYS199 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| A | SER5 | |
| I | SER5 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER58 | |
| I | SER58 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER65 | |
| I | SER65 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| A | THR83 | |
| I | THR83 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724 |
| Chain | Residue | Details |
| A | LYS205 | |
| A | LYS436 | |
| A | LYS519 | |
| A | LYS564 | |
| I | LYS205 | |
| I | LYS436 | |
| I | LYS519 | |
| I | LYS564 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724 |
| Chain | Residue | Details |
| A | SER273 | |
| I | SER273 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER419 | |
| I | SER419 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR420 | |
| A | THR422 | |
| I | THR420 | |
| I | THR422 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER489 | |
| I | SER489 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
| Chain | Residue | Details |
| A | LYS534 | |
| I | LYS534 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 |
| Chain | Residue | Details |
| A | LYS12 | |
| A | LYS281 | |
| A | LYS317 | |
| A | LYS439 | |
| I | LYS12 | |
| I | LYS281 | |
| I | LYS317 | |
| I | LYS439 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 26 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 |
| Chain | Residue | Details |
| A | LYS51 | |
| A | LYS444 | |
| A | LYS536 | |
| A | LYS545 | |
| A | LYS573 | |
| I | LYS51 | |
| I | LYS137 | |
| I | LYS162 | |
| I | LYS225 | |
| I | LYS276 | |
| I | LYS313 | |
| A | LYS137 | |
| I | LYS323 | |
| I | LYS378 | |
| I | LYS413 | |
| I | LYS444 | |
| I | LYS536 | |
| I | LYS545 | |
| I | LYS573 | |
| A | LYS162 | |
| A | LYS225 | |
| A | LYS276 | |
| A | LYS313 | |
| A | LYS323 | |
| A | LYS378 | |
| A | LYS413 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480 |
| Chain | Residue | Details |
| A | LYS199 | |
| I | LYS199 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977 |
| Chain | Residue | Details |
| A | LYS233 | |
| A | LYS351 | |
| I | LYS233 | |
| I | LYS351 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill |
| Chain | Residue | Details |
| A | ASN318 | |
| I | ASN318 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook |
| Chain | Residue | Details |
| A | ASP494 | |
| I | ASP494 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| 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 |
| A | LYS525 | |
| I | LYS525 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977 |
| Chain | Residue | Details |
| A | LYS534 | |
| I | LYS534 |
