1BTK
PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT R28C
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | HIS143 |
A | CYS154 |
A | CYS155 |
A | CYS165 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 180 |
Chain | Residue |
B | HIS143 |
B | CYS154 |
B | CYS155 |
B | CYS165 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 181 |
Chain | Residue |
A | HOH244 |
A | HOH262 |
A | HOH267 |
B | GLU96 |
B | HOH212 |
B | HOH252 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 171 |
Chain | Residue |
A | GLU96 |
A | HOH209 |
B | HOH222 |
B | HOH232 |
B | HOH251 |
site_id | ZN1 |
Number of Residues | 5 |
Details | ZN BINDING SITE IN THE BTK MOTIF, CHAIN A. |
Chain | Residue |
A | ZN1 |
A | HIS143 |
A | CYS154 |
A | CYS155 |
A | CYS165 |
site_id | ZN2 |
Number of Residues | 5 |
Details | ZN BINDING SITE IN THE BTK MOTIF, CHAIN B. |
Chain | Residue |
B | CYS165 |
B | ZN180 |
B | HIS143 |
B | CYS154 |
B | CYS155 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | Region: {"description":"Inositol-(1,3,4,5)-tetrakisphosphate 1-binding"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10196129","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00432","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10196129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9218782","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of PH domain of Bruton's tyrosine kinase.","authors":["Murayama K.","Kato-Murayama M.","Mishima C.","Shirouzu M.","Yokoyama S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16644721","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P35991","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 130 |
Details | Domain: {"description":"PH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |