3MSH
Crystal structure of Hepatitis B X-Interacting Protein at high resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005764 | cellular_component | lysosome |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0005829 | cellular_component | cytosol |
A | 0008361 | biological_process | regulation of cell size |
A | 0009615 | biological_process | response to virus |
A | 0010628 | biological_process | positive regulation of gene expression |
A | 0019079 | biological_process | viral genome replication |
A | 0031902 | cellular_component | late endosome membrane |
A | 0032008 | biological_process | positive regulation of TOR signaling |
A | 0032757 | biological_process | positive regulation of interleukin-8 production |
A | 0032991 | cellular_component | protein-containing complex |
A | 0038202 | biological_process | TORC1 signaling |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
A | 0060090 | molecular_function | molecular adaptor activity |
A | 0061462 | biological_process | protein localization to lysosome |
A | 0071230 | biological_process | cellular response to amino acid stimulus |
A | 0071986 | cellular_component | Ragulator complex |
A | 1900182 | biological_process | positive regulation of protein localization to nucleus |
A | 1904263 | biological_process | positive regulation of TORC1 signaling |
A | 1990877 | cellular_component | FNIP-folliculin RagC/D GAP |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 998 |
Chain | Residue |
A | HIS8 |
A | ASP11 |
A | MET13 |
A | PRO16 |
A | ILE18 |
A | PG4106 |
A | HOH155 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA A 100 |
Chain | Residue |
A | CYS33 |
A | ARG34 |
A | HOH153 |
A | HOH166 |
A | GLU6 |
A | GLY32 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA A 101 |
Chain | Residue |
A | GLU68 |
A | ASP70 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE IPA A 104 |
Chain | Residue |
A | LEU55 |
A | THR56 |
A | LEU67 |
A | GLU68 |
A | SER69 |
A | ASN71 |
A | GLY72 |
A | HIS87 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 105 |
Chain | Residue |
A | THR36 |
A | LEU55 |
A | ASN71 |
A | HIS87 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PG4 A 106 |
Chain | Residue |
A | HIS8 |
A | ASP11 |
A | THR12 |
A | ASP25 |
A | LEU29 |
A | HIS79 |
A | ASP80 |
A | ILE82 |
A | HOH102 |
A | HOH142 |
A | HOH165 |
A | GOL998 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | MET1 |