3AB3
Crystal structure of p115RhoGEF RGS domain in complex with G alpha 13
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001664 | molecular_function | G protein-coupled receptor binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0007165 | biological_process | signal transduction |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007266 | biological_process | Rho protein signal transduction |
A | 0019001 | molecular_function | guanyl nucleotide binding |
A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
B | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
B | 0005737 | cellular_component | cytoplasm |
C | 0001664 | molecular_function | G protein-coupled receptor binding |
C | 0003924 | molecular_function | GTPase activity |
C | 0007165 | biological_process | signal transduction |
C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
C | 0007266 | biological_process | Rho protein signal transduction |
C | 0019001 | molecular_function | guanyl nucleotide binding |
C | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
D | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
D | 0005737 | cellular_component | cytoplasm |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | SER62 |
A | THR203 |
A | GDP401 |
A | HOH408 |
A | HOH409 |
A | ALF601 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE GDP A 401 |
Chain | Residue |
A | LYS61 |
A | SER62 |
A | THR63 |
A | SER173 |
A | LEU197 |
A | LEU198 |
A | ARG200 |
A | ASN291 |
A | LYS292 |
A | ASP294 |
A | LEU295 |
A | THR348 |
A | ALA349 |
A | ILE350 |
A | HOH381 |
A | HOH408 |
A | MG501 |
A | ALF601 |
A | GLU58 |
A | SER59 |
A | GLY60 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ALF A 601 |
Chain | Residue |
A | GLY57 |
A | GLU58 |
A | LYS61 |
A | ARG200 |
A | PRO202 |
A | THR203 |
A | VAL223 |
A | GLY224 |
A | GLY225 |
A | GLN226 |
A | GDP401 |
A | HOH408 |
A | HOH409 |
A | MG501 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 502 |
Chain | Residue |
C | HOH1 |
C | SER62 |
C | THR203 |
C | ASP222 |
C | HOH388 |
C | GDP402 |
C | ALF602 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GDP C 402 |
Chain | Residue |
C | HOH1 |
C | GLU58 |
C | SER59 |
C | GLY60 |
C | LYS61 |
C | SER62 |
C | THR63 |
C | SER173 |
C | LEU197 |
C | LEU198 |
C | ARG200 |
C | ASN291 |
C | LYS292 |
C | ASP294 |
C | LEU295 |
C | THR348 |
C | ALA349 |
C | ILE350 |
C | MG502 |
C | ALF602 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ALF C 602 |
Chain | Residue |
C | HOH1 |
C | GLY57 |
C | GLU58 |
C | LYS61 |
C | ARG200 |
C | PRO202 |
C | THR203 |
C | VAL223 |
C | GLY224 |
C | GLY225 |
C | GLN226 |
C | HOH388 |
C | GDP402 |
C | MG502 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | LIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P08754 |
Chain | Residue | Details |
A | GLY17 | |
C | GLY17 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q14344 |
Chain | Residue | Details |
A | CYS18 | |
C | CYS18 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB, ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7 |
Chain | Residue | Details |
A | GLU58 | |
A | LEU197 | |
A | ASN291 | |
A | ALA349 | |
C | GLU58 | |
C | LEU197 | |
C | ASN291 | |
C | ALA349 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX6 |
Chain | Residue | Details |
A | SER62 | |
A | THR203 | |
C | SER62 | |
C | THR203 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18940608, ECO:0007744|PDB:3CX7 |
Chain | Residue | Details |
A | SER173 | |
C | SER173 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14344 |
Chain | Residue | Details |
A | THR203 | |
C | THR203 |