Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6X3O

Co-structure of BTK kinase domain with L-005191930 inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue ULY A 701
ChainResidue
ALEU408
ATHR474
AGLU475
AMET477
AGLY480
ACYS481
AASN484
ALEU528
ASER538
AASP539
ALEU542
AGLY411
AHOH863
AHOH865
AVAL416
AALA428
ALYS430
APHE442
AMET449
ALEU460
AILE472

site_idAC2
Number of Residues7
Detailsbinding site for residue 5WE A 702
ChainResidue
ATRP395
AILE397
ATRP421
ATYR425
AVAL427
ASER453
ATYR461

site_idAC3
Number of Residues19
Detailsbinding site for residue ULY B 701
ChainResidue
BLEU408
BVAL416
BALA428
BILE429
BLYS430
BPHE442
BMET449
BLEU460
BILE472
BTHR474
BGLU475
BMET477
BGLY480
BCYS481
BLEU528
BSER538
BASP539
BHOH814
BHOH854

site_idAC4
Number of Residues8
Detailsbinding site for residue 5WE B 702
ChainResidue
BSER394
BTRP421
BTYR425
BVAL427
BSER453
BTYR461
BHOH885
BHOH936

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK
ChainResidueDetails
ALEU408-LYS430

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV
ChainResidueDetails
APHE517-VAL529

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP521
BASP521

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU408
ALYS430
BLEU408
BLYS430

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT
ChainResidueDetails
ATHR474
BTHR474

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY
ChainResidueDetails
ALEU542
BLEU542

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831
ChainResidueDetails
ATYR551
BTYR551

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER604
BSER604

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15375214
ChainResidueDetails
ATYR617
BTYR617

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15375214
ChainResidueDetails
ASER623
BSER623

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER659
BSER659

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon