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2CLQ

Structure of mitogen-activated protein kinase kinase kinase 5

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 PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE STU A1941
ChainResidue
ALEU686
ALEU810
ASER821
AHOH2047
AHOH2093
AGLY687
AVAL694
AALA707
AMET754
AGLU755
AGLN756
AVAL757
AASP807

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE STU B1941
ChainResidue
BLEU686
BGLY687
BVAL694
BALA707
BGLU755
BGLN756
BVAL757
BGLY759
BASP807
BLEU810
BSER821
BHOH2032
BHOH2056

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTYGIVYaGrdlsnqvr..........IAIK
ChainResidueDetails
ALEU686-LYS709

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKgdNVLI
ChainResidueDetails
AILE799-ILE811

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis, MELK and MAP3K6","evidences":[{"source":"PubMed","id":"11920685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17210579","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19590015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23102700","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP803
AASP807

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP803
BASP807

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP803
ALYS805

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP803
BLYS805

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP803
ALYS805
ATHR842

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP803
BLYS805
BTHR842

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN808
AASP803
ALYS805

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN808
BASP803
BLYS805

243531

PDB entries from 2025-10-22

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