1QJM
Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001503 | biological_process | ossification |
A | 0001817 | biological_process | regulation of cytokine production |
A | 0002227 | biological_process | innate immune response in mucosa |
A | 0002376 | biological_process | immune system process |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005769 | cellular_component | early endosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0006508 | biological_process | proteolysis |
A | 0006826 | biological_process | iron ion transport |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0019731 | biological_process | antibacterial humoral response |
A | 0019732 | biological_process | antifungal humoral response |
A | 0031665 | biological_process | negative regulation of lipopolysaccharide-mediated signaling pathway |
A | 0032680 | biological_process | regulation of tumor necrosis factor production |
A | 0033690 | biological_process | positive regulation of osteoblast proliferation |
A | 0042581 | cellular_component | specific granule |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0045669 | biological_process | positive regulation of osteoblast differentiation |
A | 0046872 | molecular_function | metal ion binding |
A | 0055037 | cellular_component | recycling endosome |
A | 0060349 | biological_process | bone morphogenesis |
A | 1900159 | biological_process | positive regulation of bone mineralization involved in bone maturation |
A | 1900229 | biological_process | negative regulation of single-species biofilm formation in or on host organism |
A | 1902732 | biological_process | positive regulation of chondrocyte proliferation |
A | 2000308 | biological_process | negative regulation of tumor necrosis factor (ligand) superfamily member 11 production |
A | 2001205 | biological_process | negative regulation of osteoclast development |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SM A 690 |
Chain | Residue |
A | ASP60 |
A | TYR92 |
A | TYR192 |
A | HIS253 |
A | CO3692 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SM A 691 |
Chain | Residue |
A | HIS595 |
A | CO3693 |
A | ASP395 |
A | TYR433 |
A | ARG463 |
A | TYR526 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO3 A 692 |
Chain | Residue |
A | ASP60 |
A | TYR92 |
A | ARG121 |
A | SER122 |
A | ALA123 |
A | GLY124 |
A | SM690 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CO3 A 693 |
Chain | Residue |
A | ASP395 |
A | TYR433 |
A | THR459 |
A | ARG463 |
A | THR464 |
A | ALA465 |
A | ALA466 |
A | SM691 |
Functional Information from PROSITE/UniProt
site_id | PS00205 |
Number of Residues | 10 |
Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG |
Chain | Residue | Details |
A | TYR92-GLY101 | |
A | TYR433-SER442 |
site_id | PS00206 |
Number of Residues | 17 |
Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLengaGDVAF |
Chain | Residue | Details |
A | TYR192-PHE208 | |
A | TYR526-PHE542 |
site_id | PS00207 |
Number of Residues | 31 |
Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV |
Chain | Residue | Details |
A | LYS226-VAL256 | |
A | ASP568-VAL598 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741 |
Chain | Residue | Details |
A | LYS73 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741 |
Chain | Residue | Details |
A | SER259 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | ASP60 | |
A | TYR92 | |
A | TYR192 | |
A | HIS253 | |
A | ASP395 | |
A | TYR433 | |
A | TYR526 | |
A | HIS595 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475 |
Chain | Residue | Details |
A | THR117 | |
A | ARG121 | |
A | ALA123 | |
A | GLY124 | |
A | THR459 | |
A | ARG463 | |
A | ALA465 | |
A | ALA466 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | PRO430 | |
A | ASN594 | |
A | TYR660 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN137 | |
A | ASN281 | |
A | ASN476 |