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6FNH

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with a pyrazolo[3,4-d]pyrimidine fragment of NVP-BHG712

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 Residues10
Detailsbinding site for residue DXK A 1001
ChainResidue
AILE619
AHOH1274
AALA621
AALA644
ATHR692
AGLU693
AMET695
ALEU746
AEDO1006
AHOH1212

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 1002
ChainResidue
AGLN852
AARG860
APRO862

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 1003
ChainResidue
AGLN669
AHOH1109

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 1004
ChainResidue
ATYR735
AVAL736
AHIS737
AHOH1215

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 1005
ChainResidue
ATYR791
ALYS793
AHOH1158
AHOH1208
CASP708
CEDO1003

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 1006
ChainResidue
AARG743
AASN744
AASP757
ADXK1001

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 1007
ChainResidue
AASP888
CEDO1002

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO A 1008
ChainResidue
AGLN669

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 1009
ChainResidue
ATHR795
AARG858
AHOH1180
CGLU706

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 1010
ChainResidue
ALEU714
AGLY718
AHOH1166
AHOH1173

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 1011
ChainResidue
AASP708
ATHR812
AGLU815
AHOH1138

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO A 1012
ChainResidue
AASN750
AHOH1225
AHOH1335
BGLN616
BLYS617
BTYR628

site_idAD4
Number of Residues9
Detailsbinding site for residue DXK B 1001
ChainResidue
BILE619
BALA621
BALA644
BTHR692
BGLU693
BMET695
BLEU746
BHOH1189
BHOH1250

site_idAD5
Number of Residues1
Detailsbinding site for residue EDO B 1002
ChainResidue
BASN750

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO B 1003
ChainResidue
BALA770
BILE779

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO B 1004
ChainResidue
AHOH1202
BLYS684
BTYR685
BEDO1005
BHOH1111

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO B 1005
ChainResidue
BTYR685
BEDO1004
BHOH1229

site_idAD9
Number of Residues8
Detailsbinding site for residue DXK C 1001
ChainResidue
CALA621
CGLY622
CALA644
CTHR692
CGLU693
CMET695
CLEU746
CHOH1134

site_idAE1
Number of Residues5
Detailsbinding site for residue EDO C 1002
ChainResidue
AASP888
AEDO1007
CGLN852
CARG860
CPRO862

site_idAE2
Number of Residues3
Detailsbinding site for residue EDO C 1003
ChainResidue
AEDO1005
CASP708
CGLY709

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVYkGmlktssgkkevp......VAIK
ChainResidueDetails
AILE619-LYS646

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV
ChainResidueDetails
ATYR735-VAL747

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 Residues27
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q03145","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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