4FMB
VirA-Rab1 complex structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
| E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| F | 0003924 | molecular_function | GTPase activity |
| F | 0005525 | molecular_function | GTP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AF3 B 201 |
| Chain | Residue |
| A | ARG188 |
| B | GDP202 |
| B | MG203 |
| B | HOH301 |
| B | HOH303 |
| A | GLN280 |
| B | SER20 |
| B | GLY21 |
| B | LYS24 |
| B | SER42 |
| B | THR43 |
| B | THR67 |
| B | GLY69 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDP B 202 |
| Chain | Residue |
| A | ARG188 |
| A | ARG191 |
| B | ASP19 |
| B | GLY21 |
| B | VAL22 |
| B | GLY23 |
| B | LYS24 |
| B | SER25 |
| B | CYS26 |
| B | TYR36 |
| B | ASN124 |
| B | LYS125 |
| B | ASP127 |
| B | LEU128 |
| B | SER154 |
| B | ALA155 |
| B | LYS156 |
| B | AF3201 |
| B | MG203 |
| B | HOH302 |
| B | HOH303 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 203 |
| Chain | Residue |
| B | SER25 |
| B | THR43 |
| B | AF3201 |
| B | GDP202 |
| B | HOH302 |
| B | HOH303 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AF3 D 201 |
| Chain | Residue |
| C | ARG188 |
| C | GLN280 |
| C | HOH501 |
| D | SER20 |
| D | GLY21 |
| D | LYS24 |
| D | SER42 |
| D | THR43 |
| D | THR67 |
| D | GLY69 |
| D | GDP202 |
| D | MG203 |
| D | HOH302 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP D 202 |
| Chain | Residue |
| C | ARG188 |
| C | ARG191 |
| D | ASP19 |
| D | GLY21 |
| D | VAL22 |
| D | GLY23 |
| D | LYS24 |
| D | SER25 |
| D | CYS26 |
| D | TYR36 |
| D | ASN124 |
| D | LYS125 |
| D | ASP127 |
| D | LEU128 |
| D | SER154 |
| D | ALA155 |
| D | LYS156 |
| D | AF3201 |
| D | MG203 |
| D | HOH302 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 203 |
| Chain | Residue |
| D | SER25 |
| D | THR43 |
| D | AF3201 |
| D | GDP202 |
| D | HOH301 |
| D | HOH302 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AF3 F 201 |
| Chain | Residue |
| E | ARG188 |
| E | GLN280 |
| E | HOH501 |
| F | SER20 |
| F | GLY21 |
| F | LYS24 |
| F | THR43 |
| F | THR67 |
| F | GLY69 |
| F | GDP202 |
| F | MG203 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP F 202 |
| Chain | Residue |
| F | TYR36 |
| F | ASN124 |
| F | LYS125 |
| F | ASP127 |
| F | LEU128 |
| F | SER154 |
| F | ALA155 |
| F | LYS156 |
| F | AF3201 |
| F | MG203 |
| F | HOH302 |
| E | ARG188 |
| E | ARG191 |
| F | ASP19 |
| F | GLY21 |
| F | VAL22 |
| F | GLY23 |
| F | LYS24 |
| F | SER25 |
| F | CYS26 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 203 |
| Chain | Residue |
| F | SER25 |
| F | THR43 |
| F | AF3201 |
| F | GDP202 |
| F | HOH301 |
| F | HOH302 |
Functional Information from PROSITE/UniProt
| site_id | PS00675 |
| Number of Residues | 14 |
| Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKscL |
| Chain | Residue | Details |
| B | LEU14-LEU27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 273 |
| Details | Region: {"description":"Tubulin-binding domain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 51 |
| Details | Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2FOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"(Microbial infection) O-(2-cholinephosphoryl)serine","evidences":[{"source":"PubMed","id":"21822290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22158903","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32974215","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 9 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P51153","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






