3UIV
Human serum albumin-myristate-amantadine hydrochloride complex
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 | 0036094 | molecular_function | small molecule binding |
| 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 |
| H | 0003677 | molecular_function | DNA binding |
| H | 0005504 | molecular_function | fatty acid binding |
| H | 0005507 | molecular_function | copper ion binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005576 | cellular_component | extracellular region |
| H | 0005615 | cellular_component | extracellular space |
| H | 0005634 | cellular_component | nucleus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005783 | cellular_component | endoplasmic reticulum |
| H | 0005788 | cellular_component | endoplasmic reticulum lumen |
| H | 0005794 | cellular_component | Golgi apparatus |
| H | 0008289 | molecular_function | lipid binding |
| H | 0009267 | biological_process | cellular response to starvation |
| H | 0015643 | molecular_function | toxic substance binding |
| H | 0016209 | molecular_function | antioxidant activity |
| H | 0019825 | molecular_function | oxygen binding |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0031093 | cellular_component | platelet alpha granule lumen |
| H | 0032991 | cellular_component | protein-containing complex |
| H | 0036094 | molecular_function | small molecule binding |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051087 | molecular_function | protein-folding chaperone binding |
| H | 0051902 | biological_process | negative regulation of mitochondrial depolarization |
| H | 0070062 | cellular_component | extracellular exosome |
| H | 0072562 | cellular_component | blood microparticle |
| H | 0072732 | biological_process | cellular response to calcium ion starvation |
| H | 0098869 | biological_process | cellular oxidant detoxification |
| H | 0140272 | molecular_function | exogenous protein binding |
| H | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MYR A 1001 |
| Chain | Residue |
| A | ARG117 |
| A | MET123 |
| A | TYR138 |
| A | ALA158 |
| A | TYR161 |
| A | HOH1114 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MYR A 1002 |
| Chain | Residue |
| A | TYR150 |
| A | PRO152 |
| A | LEU251 |
| A | ALA254 |
| A | ARG257 |
| A | ALA258 |
| A | SER287 |
| A | HOH1227 |
| A | LEU22 |
| A | VAL23 |
| A | LEU66 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MYR A 1003 |
| Chain | Residue |
| A | SER342 |
| A | VAL344 |
| A | ARG348 |
| A | ILE388 |
| A | MET446 |
| A | ARG485 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MYR A 1004 |
| Chain | Residue |
| A | LEU387 |
| A | TYR411 |
| A | LEU460 |
| A | SER489 |
| A | HOH1279 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MYR A 1005 |
| Chain | Residue |
| A | TYR401 |
| A | ASN405 |
| A | PHE507 |
| A | LYS525 |
| A | LEU532 |
| A | VAL547 |
| A | MET548 |
| A | PHE551 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MYR A 1006 |
| Chain | Residue |
| A | GLN196 |
| A | LEU238 |
| A | HIS242 |
| A | CYS245 |
| A | ARG257 |
| A | HOH1247 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MYR H 1001 |
| Chain | Residue |
| H | ARG117 |
| H | MET123 |
| H | TYR138 |
| H | ALA158 |
| H | TYR161 |
| H | PHE165 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MYR H 1002 |
| Chain | Residue |
| H | TYR150 |
| H | ALA254 |
| H | ARG257 |
| H | ALA258 |
| H | SER287 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MYR H 1003 |
| Chain | Residue |
| H | SER342 |
| H | VAL344 |
| H | ARG348 |
| H | ILE388 |
| H | ASN391 |
| H | MET446 |
| H | ARG485 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MYR H 1004 |
| Chain | Residue |
| H | LEU387 |
| H | TYR411 |
| H | VAL415 |
| H | SER489 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MYR H 1005 |
| Chain | Residue |
| H | TYR401 |
| H | ASN405 |
| H | PHE507 |
| H | LYS525 |
| H | ALA528 |
| H | SER579 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MYR H 1006 |
| Chain | Residue |
| H | LYS199 |
| H | PHE211 |
| H | TRP214 |
| H | LEU238 |
| H | HIS242 |
| H | MYR1007 |
| H | 3081008 |
| site_id | BC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MYR H 1007 |
| Chain | Residue |
| H | TYR150 |
| H | GLU153 |
| H | SER192 |
| H | GLN196 |
| H | HIS242 |
| H | CYS245 |
| H | ARG257 |
| H | MYR1006 |
| H | 3081008 |
| H | HOH1277 |
| H | HOH1335 |
| H | HOH1356 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 308 H 1008 |
| Chain | Residue |
| H | LEU238 |
| H | LEU260 |
| H | ILE264 |
| H | SER287 |
| H | ILE290 |
| H | ALA291 |
| H | MYR1006 |
| H | MYR1007 |
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 | |
| H | HIS3 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02769 |
| Chain | Residue | Details |
| A | GLU6 | |
| H | GLU252 | |
| H | ASP255 | |
| H | ASP259 | |
| A | ASP13 | |
| A | GLU244 | |
| A | GLU252 | |
| A | ASP255 | |
| A | ASP259 | |
| H | GLU6 | |
| H | ASP13 | |
| H | 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 | |
| H | HIS67 | |
| H | HIS247 | |
| H | ASP249 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:656055 |
| Chain | Residue | Details |
| A | LYS240 | |
| H | 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 | |
| H | LYS4 | |
| H | LYS20 | |
| A | LYS64 | |
| H | LYS41 | |
| H | LYS64 | |
| H | LYS73 | |
| H | LYS93 | |
| H | LYS106 | |
| H | LYS136 | |
| H | LYS159 | |
| H | LYS174 | |
| H | LYS181 | |
| H | LYS190 | |
| A | LYS73 | |
| H | LYS195 | |
| H | LYS205 | |
| H | LYS212 | |
| H | LYS240 | |
| H | LYS262 | |
| H | LYS274 | |
| H | LYS286 | |
| H | LYS359 | |
| H | LYS372 | |
| H | LYS389 | |
| A | LYS93 | |
| H | LYS402 | |
| H | LYS414 | |
| H | LYS432 | |
| H | LYS436 | |
| H | LYS466 | |
| H | LYS475 | |
| H | LYS500 | |
| H | LYS519 | |
| H | LYS524 | |
| H | LYS538 | |
| A | LYS106 | |
| H | LYS541 | |
| H | LYS557 | |
| H | LYS560 | |
| H | LYS564 | |
| H | LYS574 | |
| A | LYS136 | |
| A | LYS159 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Aspirin-acetylated lysine |
| Chain | Residue | Details |
| A | LYS199 | |
| H | 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 | |
| H | 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 | |
| H | 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 | |
| H | 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 | |
| H | 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 | |
| H | LYS205 | |
| H | LYS436 | |
| H | LYS519 | |
| H | LYS564 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724 |
| Chain | Residue | Details |
| A | SER273 | |
| H | SER273 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER419 | |
| H | 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 | |
| H | THR420 | |
| H | THR422 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER489 | |
| H | 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 | |
| H | 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 | |
| H | LYS12 | |
| H | LYS281 | |
| H | LYS317 | |
| H | 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 | |
| H | LYS51 | |
| H | LYS137 | |
| H | LYS162 | |
| H | LYS225 | |
| H | LYS276 | |
| H | LYS313 | |
| A | LYS137 | |
| H | LYS323 | |
| H | LYS378 | |
| H | LYS413 | |
| H | LYS444 | |
| H | LYS536 | |
| H | LYS545 | |
| H | 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 | |
| H | 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 | |
| H | LYS233 | |
| H | LYS351 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill |
| Chain | Residue | Details |
| A | ASN318 | |
| H | ASN318 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook |
| Chain | Residue | Details |
| A | ASP494 | |
| H | 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 | |
| H | 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 | |
| H | LYS534 |
