Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8PM3

Crystal structure of MAP2K6 with a covalent compound GCL94

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
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAYGVVEkMrhvpsgqi..........MAVK
ChainResidueDetails
ALEU59-LYS82

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDVKpsNVLI
ChainResidueDetails
AVAL175-ILE187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP179
BASP179
CASP179
DASP179

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU59
ALYS82
BLEU59
BLYS82
CLEU59
CLYS82
DLEU59
DLYS82

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by MAP3K; alternate => ECO:0000269|PubMed:16728640
ChainResidueDetails
AASP207
BASP207
CASP207
DASP207

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by MAP3K; alternate => ECO:0000269|PubMed:16728640
ChainResidueDetails
AASP211
BASP211
CASP211
DASP211

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon