3L0I
Complex structure of SidM/DrrA with the wild type Rab1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| C | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | HIS488 |
| A | ASN489 |
| A | ALA492 |
| A | TYR529 |
| A | LYS533 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 178 |
| Chain | Residue |
| B | GLY21 |
| B | LYS24 |
| B | SER25 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1 |
| Chain | Residue |
| C | ASN489 |
| C | ALA492 |
| C | TYR529 |
| C | HIS488 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 2 |
| Chain | Residue |
| A | HIS307 |
| C | ARG276 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 178 |
| Chain | Residue |
| D | GLY21 |
| D | VAL22 |
| D | GLY23 |
| D | LYS24 |
| D | SER25 |
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 | 28 |
| 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_FI2 |
| Number of Residues | 22 |
| 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_FI3 |
| Number of Residues | 2 |
| 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_FI4 |
| Number of Residues | 2 |
| 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_FI5 |
| Number of Residues | 2 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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_FI8 |
| Number of Residues | 2 |
| 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_FI9 |
| Number of Residues | 5 |
| 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_FI10 |
| Number of Residues | 6 |
| 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 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 17 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| B | GLN70 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| D | GLN70 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| B | GLY21 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| D | GLY21 |
