1YSX
Solution structure of domain 3 from human serum albumin complexed to an anti-apoptotic ligand directed against Bcl-xL and Bcl-2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005615 | cellular_component | extracellular space |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 4EB A 1000 |
Chain | Residue |
A | ASN391 |
A | TYR452 |
A | LEU460 |
A | HIS464 |
A | CYS392 |
A | LEU407 |
A | TYR411 |
A | LYS414 |
A | VAL415 |
A | THR422 |
A | LEU423 |
A | VAL426 |
Functional Information from PROSITE/UniProt
site_id | PS00212 |
Number of Residues | 25 |
Details | ALBUMIN_1 Albumin domain signature. FaafvekCCkaDdketCFaeegkkL |
Chain | Residue | Details |
A | PHE551-LEU575 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | SITE: Not glycated => ECO:0000269|PubMed:15047055 |
Chain | Residue | Details |
A | LYS389 | |
A | LYS524 | |
A | LYS538 | |
A | LYS541 | |
A | LYS557 | |
A | LYS560 | |
A | LYS564 | |
A | LYS574 | |
A | LYS402 | |
A | LYS414 | |
A | LYS432 | |
A | LYS436 | |
A | LYS466 | |
A | LYS475 | |
A | LYS500 | |
A | LYS519 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | SER419 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | THR420 | |
A | THR422 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724 |
Chain | Residue | Details |
A | LYS436 | |
A | LYS519 | |
A | LYS564 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER489 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | LYS534 |
site_id | SWS_FT_FI7 |
Number of Residues | 5 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 |
Chain | Residue | Details |
A | LYS413 | |
A | LYS444 | |
A | LYS536 | |
A | LYS545 | |
A | LYS573 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 |
Chain | Residue | Details |
A | LYS439 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook |
Chain | Residue | Details |
A | ASP494 |
site_id | SWS_FT_FI10 |
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 |
A | LYS525 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977 |
Chain | Residue | Details |
A | LYS534 |