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4AOJ

Human TrkA in complex with the inhibitor AZ-23

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_componentmembrane
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE V4Z A 900
ChainResidue
ALEU516
AASP596
AARG654
AASN655
ACYS656
ALEU657
AGLY667
AASP668
AHOH2036
AVAL524
AALA542
APHE589
AGLU590
ATYR591
AMET592
AARG593
AGLY595

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE V4Z B 900
ChainResidue
BLEU516
BVAL524
BALA542
BPHE589
BGLU590
BTYR591
BMET592
BARG593
BGLY595
BARG654
BASN655
BLEU657
BGLY667

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE V4Z C 900
ChainResidue
CLEU516
CVAL524
CALA542
CGLU590
CTYR591
CMET592
CGLY595
CASP596
CARG654
CASN655
CCYS656
CLEU657
CGLY667
CASP668

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1790
ChainResidue
AHIS504
ACYS579
AGLU581
CCYS501

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1791
ChainResidue
AGLU515
AGLU518
ALYS523
CHIS645

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1792
ChainResidue
ACYS501
BHIS504
BCYS579
BGLU581

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1793
ChainResidue
AHIS645
BGLU515
BGLU518
BLYS523

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1790
ChainResidue
BCYS501
CHIS504
CCYS579
CGLU581

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1791
ChainResidue
BHIS645
CGLU515
CGLU518
CLYS523

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVFlAechnllpeqdkml.....VAVK
ChainResidueDetails
ALEU516-LYS544

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
APHE646-VAL658

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYstdYYR
ChainResidueDetails
AASP674-ARG682

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP650
BASP650
CASP650

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU516
ALYS544
BLEU516
BLYS544
CLEU516
CLYS544

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Breakpoint for translocation to form TRK-T1
ChainResidueDetails
ALEU486
BLEU486
CLEU486

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Interaction with SHC1
ChainResidueDetails
ATYR496
BTYR496
CTYR496

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Interaction with PLCG1
ChainResidueDetails
ATYR791
BTYR791
CTYR791

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR496
BTYR496
CTYR496

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR676
BTYR676
CTYR676

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR680
ATYR681
BTYR680
BTYR681
CTYR680
CTYR681

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR791
BTYR791
CTYR791

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PDB entries from 2024-07-24

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