6EKK
Crystal structure of GEF domain of DENND 1A in complex with Rab GTPase Rab35-GDP bound state.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| B | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LYS6 |
| A | GLN7 |
| A | ASN8 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ASP237 |
| C | PHE45 |
| C | GLN60 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | TYR222 |
| A | TRP223 |
| A | ARG4 |
| A | GLN82 |
| A | ALA215 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | TYR110 |
| A | ARG170 |
| A | ASN171 |
| A | GLU174 |
| A | SER205 |
| A | THR208 |
| A | HOH564 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ASN171 |
| A | HIS212 |
| A | HOH585 |
| A | HOH638 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | ASN70 |
| B | ASN114 |
| B | HOH525 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | LYS6 |
| B | GLN7 |
| B | ASN8 |
| B | LYS81 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | GLU45 |
| B | VAL46 |
| B | THR49 |
| B | ARG83 |
| D | THR39 |
| D | THR40 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | GLN82 |
| B | ALA215 |
| B | TYR222 |
| B | TRP223 |
| B | TYR227 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| A | THR272 |
| B | ARG123 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | ASN70 |
| B | TYR110 |
| B | ARG170 |
| B | ASN171 |
| B | SER205 |
| B | THR208 |
| B | HOH571 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | PHE337 |
| B | GLU339 |
| B | LYS365 |
| B | HOH526 |
| B | HOH572 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 201 |
| Chain | Residue |
| C | LYS100 |
| C | HIS104 |
| C | HOH343 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 202 |
| Chain | Residue |
| C | ASN31 |
| C | THR32 |
| C | PHE33 |
| C | HOH374 |
| C | HOH381 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 203 |
| Chain | Residue |
| A | HOH634 |
| C | PHE33 |
| C | SER36 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for residue GDP C 204 |
| Chain | Residue |
| C | GLY18 |
| C | VAL19 |
| C | GLY20 |
| C | LYS21 |
| C | SER22 |
| C | SER23 |
| C | ASN120 |
| C | LYS121 |
| C | ASP123 |
| C | SER150 |
| C | ALA151 |
| C | LYS152 |
| C | HOH306 |
| C | HOH312 |
| C | HOH376 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 201 |
| Chain | Residue |
| D | CYS114 |
| D | ARG115 |
| D | GLY143 |
| D | ILE144 |
| D | HOH322 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 202 |
| Chain | Residue |
| B | ILE78 |
| D | SER36 |
| D | THR39 |
| D | GDP203 |
| D | HOH371 |
| site_id | AE1 |
| Number of Residues | 19 |
| Details | binding site for residue GDP D 203 |
| Chain | Residue |
| D | SER150 |
| D | ALA151 |
| D | LYS152 |
| D | SO4202 |
| D | HOH312 |
| D | HOH321 |
| D | HOH333 |
| D | HOH384 |
| D | HOH402 |
| D | HOH410 |
| D | GLY18 |
| D | VAL19 |
| D | GLY20 |
| D | LYS21 |
| D | SER22 |
| D | SER23 |
| D | ASN120 |
| D | LYS121 |
| D | ASP123 |
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. LLIiGDSGVGKssL |
| Chain | Residue | Details |
| C | LEU11-LEU24 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 272 |
| Details | Domain: {"description":"cDENN","evidences":[{"source":"PROSITE-ProRule","id":"PRU00304","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 156 |
| Details | Domain: {"description":"dDENN","evidences":[{"source":"PROSITE-ProRule","id":"PRU00304","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Motif: {"description":"FXDXF motif","evidences":[{"source":"PubMed","id":"20154091","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"30905672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"30905672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30905672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30905672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IF2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by LRRK2","evidences":[{"source":"PubMed","id":"29125462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-(2-cholinephosphoryl)serine","evidences":[{"source":"PubMed","id":"21822290","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22307087","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-AMP-tyrosine","evidences":[{"source":"PubMed","id":"21822290","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






