6FIT
FHIT-TRANSITION STATE ANALOG
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001650 | cellular_component | fibrillar center |
A | 0003824 | molecular_function | catalytic activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006163 | biological_process | purine nucleotide metabolic process |
A | 0006915 | biological_process | apoptotic process |
A | 0015964 | biological_process | diadenosine triphosphate catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0031625 | molecular_function | ubiquitin protein ligase binding |
A | 0032435 | biological_process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
A | 0047352 | molecular_function | adenylylsulfate-ammonia adenylyltransferase activity |
A | 0047627 | molecular_function | adenylylsulfatase activity |
A | 0047710 | molecular_function | bis(5'-adenosyl)-triphosphatase activity |
A | 0072332 | biological_process | intrinsic apoptotic signaling pathway by p53 class mediator |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMW A 148 |
Chain | Residue |
A | ASN27 |
A | ARG28 |
A | GLN83 |
A | GLY89 |
A | GLN90 |
A | THR91 |
A | VAL92 |
A | HIS96 |
A | HIS98 |
A | HOH150 |
A | HOH172 |
A | PHE5 |
A | HIS8 |
A | ILE10 |
A | LEU25 |
A | VAL26 |
site_id | AVE |
Number of Residues | 1 |
Details | ACTIVE SITE HISTIDINE RESPONSIBLE FOR FORMING THE TRANSIENT NUCLEOTIDYL PHOSPHOHISTIDYL ENZYME INTERMEDIATE DURING CATALYSIS. IN THIS STRUCTURE, IT IS COVALENTLY ASSOCIATED WITH THE AMW RESIDUE WHICH CONSISTS OF AN ADENOSINE BASE AND A PENTACOVALENT TUNGSTATE ION. |
Chain | Residue |
A | HIS96 |
site_id | HNE |
Number of Residues | 3 |
Details | HISTIDINE TRIAD FOR WHICH THIS FAMILY WAS NAMED. |
Chain | Residue |
A | HIS35 |
A | HIS96 |
A | HIS98 |
Functional Information from PROSITE/UniProt
site_id | PS00892 |
Number of Residues | 19 |
Details | HIT_1 HIT domain signature. QdgpeAgQtVkHVHVHVLP |
Chain | Residue | Details |
A | GLN83-PRO101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:15182206, ECO:0000269|PubMed:9323207 |
Chain | Residue | Details |
A | HIS96 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9261067, ECO:0007744|PDB:3FIT |
Chain | Residue | Details |
A | HIS8 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9323207, ECO:0007744|PDB:5FIT |
Chain | Residue | Details |
A | ASN27 | |
A | GLN83 | |
A | GLY89 | |
A | HIS98 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for induction of apoptosis => ECO:0000269|PubMed:16407838 |
Chain | Residue | Details |
A | TYR114 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:15007172 |
Chain | Residue | Details |
A | TYR114 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15007172 |
Chain | Residue | Details |
A | TYR145 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 5fit |
Chain | Residue | Details |
A | GLN83 | |
A | HIS96 | |
A | HIS94 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 101 |
Chain | Residue | Details |
A | GLN83 | electrostatic stabiliser, hydrogen bond donor |
A | HIS94 | electrostatic stabiliser, increase electrophilicity, increase nucleophilicity |
A | HIS96 | metal ligand, nucleofuge, nucleophile |
A | HIS98 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |