1MQB

Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

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
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ANP A 1000

Chain	Residue
A	ALA621
A	GLY622
A	ALA644
A	LYS646
A	THR692
A	GLU693
A	TYR694
A	MET695
A	LEU746

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP B 1001

Chain	Residue
B	HOH310
B	ILE619
B	GLY622
B	GLU623
B	ALA644
B	LYS646
B	THR692
B	GLU693
B	MET695
B	ASN744
B	LEU746
B	ASP757

---

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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP739
B	ASP739

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE619
A	LYS646
B	ILE619
B	LYS646

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR628
B	TYR628

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR647
B	THR647

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q03145

Chain	Residue	Details
A	TYR735
B	TYR735

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q03145

Chain	Residue	Details
A	TYR772
B	TYR772

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER869
B	SER869

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER892
B	SER892

---

site_id	SWS_FT_FI9
Number of Residues	2
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
B	SER897

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG743
A	ASP739

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ARG743
B	ASP739

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA741
A	ASP739

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ALA741
B	ASP739

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA741
A	ASN744
A	ASP739

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ALA741
B	ASN744
B	ASP739

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