3GC8
The structure of p38beta C162S in complex with a dihydroquinazolinone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000165 | biological_process | MAPK cascade |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001649 | biological_process | osteoblast differentiation |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004707 | molecular_function | MAP kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0031098 | biological_process | stress-activated protein kinase signaling cascade |
| A | 0032735 | biological_process | positive regulation of interleukin-12 production |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0038066 | biological_process | p38MAPK cascade |
| A | 0045648 | biological_process | positive regulation of erythrocyte differentiation |
| A | 0051149 | biological_process | positive regulation of muscle cell differentiation |
| A | 0051403 | biological_process | stress-activated MAPK cascade |
| A | 0060348 | biological_process | bone development |
| A | 0071347 | biological_process | cellular response to interleukin-1 |
| A | 0071493 | biological_process | cellular response to UV-B |
| A | 0090398 | biological_process | cellular senescence |
| A | 0098586 | biological_process | cellular response to virus |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0000165 | biological_process | MAPK cascade |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001649 | biological_process | osteoblast differentiation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004707 | molecular_function | MAP kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0010628 | biological_process | positive regulation of gene expression |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0031098 | biological_process | stress-activated protein kinase signaling cascade |
| B | 0032735 | biological_process | positive regulation of interleukin-12 production |
| B | 0035556 | biological_process | intracellular signal transduction |
| B | 0038066 | biological_process | p38MAPK cascade |
| B | 0045648 | biological_process | positive regulation of erythrocyte differentiation |
| B | 0051149 | biological_process | positive regulation of muscle cell differentiation |
| B | 0051403 | biological_process | stress-activated MAPK cascade |
| B | 0060348 | biological_process | bone development |
| B | 0071347 | biological_process | cellular response to interleukin-1 |
| B | 0071493 | biological_process | cellular response to UV-B |
| B | 0090398 | biological_process | cellular senescence |
| B | 0098586 | biological_process | cellular response to virus |
| B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 601 |
| Chain | Residue |
| A | HIS64 |
| A | GLU81 |
| A | ASP316 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE B45 A 365 |
| Chain | Residue |
| A | LEU104 |
| A | THR106 |
| A | THR107 |
| A | LEU108 |
| A | MET109 |
| A | GLY110 |
| A | ALA111 |
| A | SER154 |
| A | ALA157 |
| A | LEU167 |
| A | VAL30 |
| A | TYR35 |
| A | VAL38 |
| A | ALA51 |
| A | VAL52 |
| A | LYS53 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI B 602 |
| Chain | Residue |
| A | HIS199 |
| B | GLU245 |
| B | ASP292 |
| B | ASP294 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 603 |
| Chain | Residue |
| B | HIS64 |
| B | GLU81 |
| B | ASP316 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE B45 B 365 |
| Chain | Residue |
| B | VAL30 |
| B | TYR35 |
| B | VAL38 |
| B | ALA51 |
| B | VAL52 |
| B | LYS53 |
| B | LEU104 |
| B | THR106 |
| B | THR107 |
| B | LEU108 |
| B | MET109 |
| B | GLY110 |
| B | ALA111 |
| B | SER154 |
| B | ALA157 |
| B | LEU167 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCsAydarlrqkv.........AVKK |
| Chain | Residue | Details |
| A | VAL30-LYS54 |
| site_id | PS01351 |
| Number of Residues | 104 |
| Details | MAPK MAP kinase signature. FqsliharrtyRElrllkhlkhenviglldvftpatsiedfsevylvttlmgadlnnivkcqalsdehvqflvyqllrglkyihsagiih.........RDlKpsnvavnedS |
| Chain | Residue | Details |
| A | PHE59-SER162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 568 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Motif: {"description":"TXY"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K6","evidences":[{"source":"PubMed","id":"38270553","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15356147","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K6","evidences":[{"source":"PubMed","id":"38270553","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15356147","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by ZAP70","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER154 | |
| A | ASP150 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | SER154 | |
| B | ASP150 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS152 | |
| A | ASP150 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS152 | |
| B | ASP150 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS152 | |
| A | THR185 | |
| A | ASP150 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS152 | |
| B | THR185 | |
| B | ASP150 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN155 | |
| A | LYS152 | |
| A | ASP150 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN155 | |
| B | LYS152 | |
| B | ASP150 |
