4HLQ
Crystal structure of human rab1b bound to GDP and BEF3 in complex with the GAP domain of TBC1D20 from homo sapiens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005096 | molecular_function | GTPase activator activity |
| A | 0016192 | biological_process | vesicle-mediated transport |
| A | 0043547 | biological_process | positive regulation of GTPase activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| C | 0005096 | molecular_function | GTPase activator activity |
| C | 0016192 | biological_process | vesicle-mediated transport |
| C | 0043547 | biological_process | positive regulation of GTPase activity |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
| E | 0005096 | molecular_function | GTPase activator activity |
| E | 0016192 | biological_process | vesicle-mediated transport |
| E | 0043547 | biological_process | positive regulation of GTPase activity |
| F | 0003924 | molecular_function | GTPase activity |
| F | 0005525 | molecular_function | GTP binding |
| G | 0005096 | molecular_function | GTPase activator activity |
| G | 0016192 | biological_process | vesicle-mediated transport |
| G | 0043547 | biological_process | positive regulation of GTPase activity |
| H | 0003924 | molecular_function | GTPase activity |
| H | 0005525 | molecular_function | GTP binding |
| I | 0005096 | molecular_function | GTPase activator activity |
| I | 0016192 | biological_process | vesicle-mediated transport |
| I | 0043547 | biological_process | positive regulation of GTPase activity |
| J | 0003924 | molecular_function | GTPase activity |
| J | 0005525 | molecular_function | GTP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG67 |
| A | ARG160 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 201 |
| Chain | Residue |
| B | SER22 |
| B | THR40 |
| B | ASP63 |
| B | THR64 |
| B | GDP202 |
| B | BEF203 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 202 |
| Chain | Residue |
| B | SER17 |
| B | GLY18 |
| B | GLY20 |
| B | LYS21 |
| B | SER22 |
| B | CYS23 |
| B | TYR33 |
| B | GLU35 |
| B | SER36 |
| B | THR40 |
| B | ASN121 |
| B | LYS122 |
| B | ASP124 |
| B | LEU125 |
| B | ALA152 |
| B | LYS153 |
| B | MG201 |
| B | BEF203 |
| A | ARG105 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF B 203 |
| Chain | Residue |
| A | ARG105 |
| A | GLN144 |
| B | SER17 |
| B | LYS21 |
| B | THR40 |
| B | THR64 |
| B | ALA65 |
| B | GLY66 |
| B | MG201 |
| B | GDP202 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 401 |
| Chain | Residue |
| A | ASN88 |
| C | SER293 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| D | SER22 |
| D | THR40 |
| D | GDP202 |
| D | BEF203 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDP D 202 |
| Chain | Residue |
| C | ARG105 |
| D | GLY18 |
| D | VAL19 |
| D | GLY20 |
| D | LYS21 |
| D | SER22 |
| D | CYS23 |
| D | TYR33 |
| D | GLU35 |
| D | ASN121 |
| D | LYS122 |
| D | ASP124 |
| D | LEU125 |
| D | ALA152 |
| D | LYS153 |
| D | MG201 |
| D | BEF203 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF D 203 |
| Chain | Residue |
| C | ARG105 |
| C | GLN144 |
| D | SER17 |
| D | LYS21 |
| D | SER22 |
| D | THR40 |
| D | THR64 |
| D | GLY66 |
| D | MG201 |
| D | GDP202 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 E 401 |
| Chain | Residue |
| E | ARG160 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 E 402 |
| Chain | Residue |
| E | ARG175 |
| H | GLN104 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 201 |
| Chain | Residue |
| F | SER22 |
| F | THR40 |
| F | GDP202 |
| F | BEF203 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GDP F 202 |
| Chain | Residue |
| E | ARG105 |
| F | GLY18 |
| F | VAL19 |
| F | GLY20 |
| F | LYS21 |
| F | SER22 |
| F | CYS23 |
| F | TYR33 |
| F | GLU35 |
| F | ASN121 |
| F | LYS122 |
| F | ASP124 |
| F | LEU125 |
| F | SER151 |
| F | ALA152 |
| F | LYS153 |
| F | MG201 |
| F | BEF203 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF F 203 |
| Chain | Residue |
| F | LYS21 |
| F | THR40 |
| F | THR64 |
| F | GLY66 |
| F | MG201 |
| F | GDP202 |
| E | ARG105 |
| E | GLN144 |
| F | SER17 |
| F | GLY18 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG H 201 |
| Chain | Residue |
| H | SER22 |
| H | THR40 |
| H | GDP202 |
| H | BEF203 |
| site_id | BC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GDP H 202 |
| Chain | Residue |
| G | ARG105 |
| H | GLY18 |
| H | VAL19 |
| H | GLY20 |
| H | LYS21 |
| H | SER22 |
| H | CYS23 |
| H | TYR33 |
| H | GLU35 |
| H | SER36 |
| H | ASN121 |
| H | ASP124 |
| H | ALA152 |
| H | LYS153 |
| H | MG201 |
| H | BEF203 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF H 203 |
| Chain | Residue |
| G | ARG105 |
| G | GLN144 |
| H | SER17 |
| H | LYS21 |
| H | THR40 |
| H | THR64 |
| H | ALA65 |
| H | GLY66 |
| H | MG201 |
| H | GDP202 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 I 401 |
| Chain | Residue |
| I | PRO287 |
| I | TYR288 |
| I | GLU289 |
| I | THR290 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG J 201 |
| Chain | Residue |
| J | SER22 |
| J | THR40 |
| J | GDP202 |
| J | BEF203 |
| site_id | CC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDP J 202 |
| Chain | Residue |
| I | ARG105 |
| J | ASP16 |
| J | SER17 |
| J | GLY18 |
| J | VAL19 |
| J | GLY20 |
| J | LYS21 |
| J | SER22 |
| J | CYS23 |
| J | TYR33 |
| J | GLU35 |
| J | THR40 |
| J | ASN121 |
| J | LYS122 |
| J | ASP124 |
| J | SER151 |
| J | ALA152 |
| J | LYS153 |
| J | MG201 |
| J | BEF203 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEF J 203 |
| Chain | Residue |
| I | ARG105 |
| I | GLN144 |
| J | SER17 |
| J | GLY18 |
| J | THR40 |
| J | GLY66 |
| J | MG201 |
| J | GDP202 |
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 | LEU11-LEU24 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20064470, ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3JZA, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
| Chain | Residue | Details |
| B | GLY15 | |
| D | GLY15 | |
| F | GLY15 | |
| H | GLY15 | |
| J | GLY15 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
| Chain | Residue | Details |
| B | TYR33 | |
| D | TYR33 | |
| F | TYR33 | |
| H | TYR33 | |
| J | TYR33 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
| Chain | Residue | Details |
| B | ASP63 | |
| D | ASP63 | |
| F | ASP63 | |
| H | ASP63 | |
| J | ASP63 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
| Chain | Residue | Details |
| B | ASN121 | |
| J | SER151 | |
| B | SER151 | |
| D | ASN121 | |
| D | SER151 | |
| F | ASN121 | |
| F | SER151 | |
| H | ASN121 | |
| H | SER151 | |
| J | ASN121 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | MOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087 |
| Chain | Residue | Details |
| B | SER76 | |
| D | SER76 | |
| F | SER76 | |
| H | SER76 | |
| J | SER76 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 5 |
| Details | MOD_RES: (Microbial infection) O-AMP-tyrosine => ECO:0000269|PubMed:20651120 |
| Chain | Residue | Details |
| B | TYR77 | |
| D | TYR77 | |
| F | TYR77 | |
| H | TYR77 | |
| J | TYR77 |
