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2XUU

Crystal structure of a DAP-kinase 1 mutant

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 Residues19
DetailsBINDING SITE FOR RESIDUE ADP A 1303
ChainResidue
AGLY20
AMG1307
AHOH2048
AHOH2121
AHOH2232
AHOH2234
AHOH2398
AHOH2400
AHOH2401
AHOH2402
AHOH2403
ASER21
AGLY22
AVAL27
ALYS42
AGLU94
AVAL96
AILE160
AASP161

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1304
ChainResidue
AARG47
ALYS50
ASER57
AARG58
AHOH2404
AHOH2405
AHOH2406
AHOH2407

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1305
ChainResidue
AARG47
ALYS249
AARG253
AHOH2106

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1306
ChainResidue
AARG150
AASN151
AHOH2174
AHOH2175
AHOH2241
AHOH2351
AHOH2408

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1307
ChainResidue
AASP161
AADP1303
AHOH2223
AHOH2234
AHOH2402

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......FIKK
ChainResidueDetails
ALEU19-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML
ChainResidueDetails
AILE135-LEU147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP139

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS42
AGLU94
AGLU100
AASP161
ALEU19

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by RPS6KA1 and RPS6KA3 => ECO:0000269|PubMed:16213824
ChainResidueDetails
ASER289

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11579085, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602
ChainResidueDetails
ASER308

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER319

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER333

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PDB entries from 2024-06-12

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