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8D6C

Crystal Structure of Human Myt1 Kinase domain Bounded with compound 28

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGSYGEVFkVrskedgrl..........YAVK
ChainResidueDetails
ALEU116-LYS139

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHlDVKpaNIFL
ChainResidueDetails
ALEU229-LEU241

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:PRU10027
ChainResidueDetails
AASP233
BASP233

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU116
ALYS139
BLEU116
BLYS139

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30291
ChainResidueDetails
AASN238
AASP251
AGLY253
BASN238
BASP251
BGLY253

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER94
BSER94

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER120
BSER120

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER143
BSER143

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER160
BSER160

222036

PDB entries from 2024-07-03

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