2QO7

Human EphA3 kinase and juxtamembrane region, dephosphorylated, AMP-PNP bound

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	4
Details	BINDING SITE FOR RESIDUE MG A 1

Chain	Residue
A	ANP1000
A	HOH1081
A	HOH1094
A	HOH1224

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 948

Chain	Residue
A	GLU634
A	CYS636
A	ILE652
A	THR654

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP A 1000

Chain	Residue
A	ALA629
A	GLY630
A	GLU631
A	ALA651
A	LYS653
A	THR699
A	GLU700
A	MET702
A	SER706
A	LEU753
A	HOH1081
A	HOH1119
A	HOH1155
A	HOH1189
A	HOH1191
A	HOH1196
A	HOH1224
A	MG1

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 1001

Chain	Residue
A	THR719

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 2

Chain	Residue
A	GLN717
A	LYS735
A	GLU872
A	HOH1135
A	HOH1156

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGAGEFGEVCsGrlklpskkeis.......VAIK

Chain	Residue	Details
A	VAL627-LYS653

---

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

Chain	Residue	Details
A	TYR742-ILE754

---

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	ASP746

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	GLY628
A	LYS653
A	GLU700
A	ARG750

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:18547520

Chain	Residue	Details
A	TYR596
A	TYR602

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18547520

Chain	Residue	Details
A	PTR701

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11870224

Chain	Residue	Details
A	TYR779

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P29319

Chain	Residue	Details
A	TYR937

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG750
A	ASP746

---

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

Chain	Residue	Details
A	ASP746
A	ALA748

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP746
A	ASN751
A	ALA748

---