4EMX
Crystal structure analysis of Human Serum Albumin in complex with chloride anions at cryogenic temperature
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 |
| 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 | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009267 | biological_process | cellular response to starvation |
| B | 0015643 | molecular_function | toxic substance binding |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031093 | cellular_component | platelet alpha granule lumen |
| B | 0032991 | cellular_component | protein-containing complex |
| 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 | 0140272 | molecular_function | exogenous protein binding |
| B | 1903981 | molecular_function | enterobactin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | LYS190 |
| A | LYS432 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 602 |
| Chain | Residue |
| A | LEU238 |
| A | HIS242 |
| A | HOH718 |
| A | HOH811 |
| A | HOH822 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 603 |
| Chain | Residue |
| A | TYR411 |
| A | SER489 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 601 |
| Chain | Residue |
| B | TYR411 |
| B | SER489 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 602 |
| Chain | Residue |
| B | LYS199 |
| B | TRP214 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 603 |
| Chain | Residue |
| B | TYR150 |
| B | ARG257 |
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 | |
| B | HIS3 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02769 |
| Chain | Residue | Details |
| A | GLU6 | |
| B | GLU252 | |
| B | ASP255 | |
| B | ASP259 | |
| A | ASP13 | |
| A | GLU244 | |
| A | GLU252 | |
| A | ASP255 | |
| A | ASP259 | |
| B | GLU6 | |
| B | ASP13 | |
| B | 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 | |
| B | HIS67 | |
| B | HIS247 | |
| B | ASP249 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:656055 |
| Chain | Residue | Details |
| A | LYS240 | |
| B | 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 | |
| B | LYS4 | |
| B | LYS20 | |
| A | LYS64 | |
| B | LYS41 | |
| B | LYS64 | |
| B | LYS73 | |
| B | LYS93 | |
| B | LYS106 | |
| B | LYS136 | |
| B | LYS159 | |
| B | LYS174 | |
| B | LYS181 | |
| B | LYS190 | |
| A | LYS73 | |
| B | LYS195 | |
| B | LYS205 | |
| B | LYS212 | |
| B | LYS240 | |
| B | LYS262 | |
| B | LYS274 | |
| B | LYS286 | |
| B | LYS359 | |
| B | LYS372 | |
| B | LYS389 | |
| A | LYS93 | |
| B | LYS402 | |
| B | LYS414 | |
| B | LYS432 | |
| B | LYS436 | |
| B | LYS466 | |
| B | LYS475 | |
| B | LYS500 | |
| B | LYS519 | |
| B | LYS524 | |
| B | LYS538 | |
| A | LYS106 | |
| B | LYS541 | |
| B | LYS557 | |
| B | LYS560 | |
| B | LYS564 | |
| B | LYS574 | |
| A | LYS136 | |
| A | LYS159 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Aspirin-acetylated lysine |
| Chain | Residue | Details |
| A | LYS199 | |
| B | 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 | |
| B | 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 | |
| B | 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 | |
| B | 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 | |
| B | 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 | |
| B | LYS205 | |
| B | LYS436 | |
| B | LYS519 | |
| B | LYS564 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724 |
| Chain | Residue | Details |
| A | SER273 | |
| B | SER273 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER419 | |
| B | 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 | |
| B | THR420 | |
| B | THR422 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER489 | |
| B | 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 | |
| B | 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 | |
| B | LYS12 | |
| B | LYS281 | |
| B | LYS317 | |
| B | 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 | |
| B | LYS51 | |
| B | LYS137 | |
| B | LYS162 | |
| B | LYS225 | |
| B | LYS276 | |
| B | LYS313 | |
| A | LYS137 | |
| B | LYS323 | |
| B | LYS378 | |
| B | LYS413 | |
| B | LYS444 | |
| B | LYS536 | |
| B | LYS545 | |
| B | 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 | |
| B | 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 | |
| B | LYS233 | |
| B | LYS351 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill |
| Chain | Residue | Details |
| A | ASN318 | |
| B | ASN318 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook |
| Chain | Residue | Details |
| A | ASP494 | |
| B | 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 | |
| B | 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 | |
| B | LYS534 |
