6FNG

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with an isomer of NVP-BHG712

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue DWT A 1001

Chain	Residue
A	VAL627
A	MET695
A	LEU730
A	TYR735
A	LEU746
A	VAL755
A	SER756
A	ASP757
A	PHE758
A	HOH1219
A	HOH1225
A	ALA644
A	LYS646
A	GLU663
A	MET667
A	PHE670
A	ILE675
A	THR692
A	TYR694

---

site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 1002

Chain	Residue
A	ILE781
A	THR784
A	ILE789
A	MET827
A	EDO1004
A	HOH1115

---

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 1003

Chain	Residue
A	ASN732
A	GLU815
A	LYS863
A	PHE864
A	ALA865
A	HOH1133

---

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 1004

Chain	Residue
A	GLU710
A	PRO786
A	SER790
A	ASN831
A	EDO1002

---

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 1005

Chain	Residue
A	GLY709
A	GLU710
A	PHE711
A	SER712
A	ASN831

---

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 1006

Chain	Residue
A	GLU706
A	LYS707
A	GLU710
A	SER790
A	HOH1251

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVYkGmlktssgkkevp......VAIK

Chain	Residue	Details
A	ILE619-LYS646

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV

Chain	Residue	Details
A	TYR735-VAL747

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP739

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS646
A	ILE619

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR628

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR647

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q03145

Chain	Residue	Details
A	TYR735

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q03145

Chain	Residue	Details
A	TYR772

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER869

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER892

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKB/AKT1, RPS6KA1, RPS6KA3 AND PKA => ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:26158630, ECO:0000269|PubMed:27385333, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER897

---