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

2C30

Crystal Structure Of The Human P21-Activated Kinase 6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A1675
ChainResidue
AGLN444
AARG445
AARG446
AHOH2349
AHOH2350

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1676
ChainResidue
AGLN485
ATHR535
ALEU536

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVClArekhsgrq..........VAVK
ChainResidueDetails
AILE413-LYS436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP526

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE413
ALYS436

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
ASEP560

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP530
AASP526

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS528
AASP526

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS528
ATHR564
AASP526

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER531
ALYS528
AASP526

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon