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3BCE

Crystal structure of the ErbB4 kinase

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
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN A 1
ChainResidue
ATHR901
CTHR901

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 C 502
ChainResidue
CGLN793
CASN797
CASN830

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG C 501
ChainResidue
CMET774
CLEU825
CTHR835
CMET747
CVAL756
CTHR771
CGLN772

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGiwvpegetvkip......VAIK
ChainResidueDetails
ALEU699-LYS726

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV
ChainResidueDetails
ALEU814-VAL826

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"18721752","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP818
AARG822

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP818
BARG822

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP818
CARG822

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP818
AALA820

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP818
BALA820

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP818
CALA820

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN823
AASP818
AALA820

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN823
BASP818
BALA820

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN823
CASP818
CALA820

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PDB entries from 2025-11-05

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