3VNT

Crystal Structure of the Kinase domain of Human VEGFR2 with a [1,3]thiazolo[5,4-b]pyridine derivative

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	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 0JA A 2001

Chain	Residue
A	VAL848
A	VAL916
A	GLU917
A	PHE918
A	CYS919
A	LYS920
A	GLY922
A	LEU1019
A	LEU1035
A	ILE1044
A	CYS1045
A	ALA866
A	ASP1046
A	PHE1047
A	EDO2002
A	HOH3072
A	HOH3221
A	LYS868
A	GLU885
A	LEU889
A	ILE892
A	VAL898
A	VAL899
A	VAL914

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 2002

Chain	Residue
A	GLY922
A	ASN923
A	PHE1047
A	0JA2001
A	HOH3120
A	HOH3136

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 2003

Chain	Residue
A	ALA1020
A	GLN1085
A	THR1152
A	PHE1153
A	SER1154
A	HOH3092
A	HOH3121

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 2004

Chain	Residue
A	TRP1096
A	SER1100
A	PRO1128
A	ASP1129
A	HOH3009

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAFGQVIeAdafgidktatcrt.....VAVK

Chain	Residue	Details
A	LEU840-LYS868

---

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

Chain	Residue	Details
A	CYS1024-LEU1036

---

site_id	PS00240
Number of Residues	14
Details	RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GhHlNVVNLLGACT

Chain	Residue	Details
A	GLY893-THR906

---

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	PHE1078

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LEU840
A	LYS868

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19136612

Chain	Residue	Details
A	THR1001

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	ARG1032
A	ILE1034

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:18936167

Chain	Residue	Details
A	ASP1046

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10037737, ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167

Chain	Residue	Details
A	SER1104

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10037737, ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:10368301, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167

Chain	Residue	Details
A	VAL1109

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