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2P0C

Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 4
ChainResidue
AANP1
AASN728
AASP741

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 5
ChainResidue
BANP2
BHOH129
BASN728
BASP741

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 6
ChainResidue
BGLU712
BASN716

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP A 1
ChainResidue
AMG4
AHOH82
AHOH84
AHOH113
AHOH121
AHOH141
ALEU593
AGLY594
AVAL601
AALA617
APRO672
APHE673
AMET674
AASP723
AARG727
AASN728
AMET730
AASP741

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP B 2
ChainResidue
BMG5
BHOH51
BHOH66
BHOH83
BHOH129
BHOH156
BHOH163
BHOH170
BLEU593
BVAL601
BALA617
BPRO672
BPHE673
BMET674
BASP678
BARG727
BASP741

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 3
ChainResidue
ALEU697
AALA794
AARG796
ACYS825
ALEU829

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGSVMeGnlkqedgtslk.......VAVK
ChainResidueDetails
ALEU593-LYS619

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCML
ChainResidueDetails
APHE719-LEU731

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP723
BASP723

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU593
ALYS615
BLEU593
BLYS615

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8702477
ChainResidueDetails
ATYR749
ATYR753
ATYR754
BTYR749
BTYR753
BTYR754

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG727
AASP723

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG727
BASP723

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA725
AASP723

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA725
BASP723

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA725
AASN728
AASP723

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA725
BASN728
BASP723

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PDB entries from 2024-07-24

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