3V89
The crystal structure of transferrin binding protein A (TbpA) from Neisseria meningitidis serogroup B in complex with the C-lobe of 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 | 0019867 | cellular_component | outer membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0033214 | biological_process | siderophore-iron import into cell |
| A | 0034755 | biological_process | iron ion transmembrane transport |
| A | 0044718 | biological_process | siderophore transmembrane transport |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YfAVAVVKKS |
| Chain | Residue | Details |
| B | TYR426-SER435 |
| site_id | PS00206 |
| Number of Residues | 16 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLvek.GDVAF |
| Chain | Residue | Details |
| B | TYR517-PHE532 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DYeLLClDgtrkp...VeeyanChlArapnHaVV |
| Chain | Residue | Details |
| 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. NryaApGRnYtFSLeMkF |
| Chain | Residue | Details |
| A | ASN898-PHE915 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Motif: {"description":"TonB C-terminal box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 193 |
| Details | Transmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 451 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 25 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 125 |
| Details | Domain: {"description":"TBDR plug","evidences":[{"source":"PROSITE-ProRule","id":"PRU01360","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | Region: {"description":"Plug loop, interacts with transferrin","evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 10 |
| Details | Region: {"description":"L3 helix finger, interacts with transferrin","evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 322 |
| Details | Domain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000074","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000075","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
