3V8X
The crystal structure of transferrin binding protein A (TbpA) from Neisserial meningitidis serogroup B in complex with full length human transferrin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006826 | biological_process | iron ion transport |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0015091 | molecular_function | ferric iron transmembrane transporter activity |
| A | 0015344 | molecular_function | siderophore uptake transmembrane transporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0019867 | cellular_component | outer membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0033214 | biological_process | siderophore-dependent iron import into cell |
| A | 0044718 | biological_process | siderophore transmembrane transport |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0008199 | molecular_function | ferric iron binding |
Functional Information from PROSITE/UniProt
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
| Chain | Residue | Details |
| B | GLN222-VAL252 | |
| B | ASP558-VAL588 |
| site_id | PS00430 |
| Number of Residues | 34 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mdihhhhhhhhhhenvqagqaqekql.........................................................................................DTIQVKAK |
| Chain | Residue | Details |
| A | MET12-LYS45 |
| site_id | PS01156 |
| Number of Residues | 18 |
| Details | TONB_DEPENDENT_REC_2 TonB-dependent receptor (TBDR) proteins signature 2. NryaApGRnYtFSLeYkF |
| Chain | Residue | Details |
| A | ASN898-PHE915 |
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD |
| Chain | Residue | Details |
| B | TYR95-ASP104 | |
| B | TYR426-SER435 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
| Chain | Residue | Details |
| B | TYR188-PHE204 | |
| B | TYR517-PHE532 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83 |
| Chain | Residue | Details |
| B | ASP63 | |
| A | PRO800-GLY802 | |
| A | VAL856-PHE860 | |
| B | TYR95 | |
| B | TYR188 | |
| B | HIS249 | |
| A | ASP489-ARG494 | |
| A | GLY593-ARG594 | |
| A | PRO634-TRP637 | |
| A | GLY686-GLY689 | |
| A | TRP744-TRP755 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | THR120 | |
| A | ALA584-LEU592 | |
| A | TRP595-ARG603 | |
| A | LEU624-LYS633 | |
| A | LEU638-GLY647 | |
| A | PHE676-LYS685 | |
| A | ASN690-ALA699 | |
| A | THR734-ASP743 | |
| A | TYR756-ARG765 | |
| A | TYR791-GLN799 | |
| A | LYS803-THR811 | |
| B | ARG124 | |
| A | TYR846-THR855 | |
| A | THR861-LEU870 | |
| A | ASN906-PHE915 | |
| B | ALA126 | |
| B | GLY127 | |
| A | HIS325-THR334 | |
| A | ARG407-THR415 | |
| A | ASP424-GLN433 | |
| A | LEU479-PHE488 | |
| A | HIS495-ASP504 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ |
| Chain | Residue | Details |
| B | ASP392 | |
| A | TYR812-TRP845 | |
| A | ASN871-ARG905 | |
| B | TYR426 | |
| B | TYR517 | |
| B | HIS585 | |
| A | ARG505-TYR583 | |
| A | TYR604-THR623 | |
| A | PHE648-SER675 | |
| A | TYR700-ILE733 | |
| A | VAL766-ARG790 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741 |
| Chain | Residue | Details |
| B | THR452 | |
| B | ARG456 | |
| B | ALA458 | |
| B | GLY459 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346 |
| Chain | Residue | Details |
| B | ARG23 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| B | SER370 | |
| B | SER666 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc...) serine |
| Chain | Residue | Details |
| B | SER32 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ |
| Chain | Residue | Details |
| B | ASN413 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627 |
| Chain | Residue | Details |
| B | ASN472 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295 |
| Chain | Residue | Details |
| B | ASN611 |
