3LVP

Crystal structure of bisphosphorylated IGF1-R Kinase domain (2P) in complex with a bis-azaindole inhibitor

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
A	0016020	cellular_component	membrane
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
B	0016020	cellular_component	membrane
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
C	0016020	cellular_component	membrane
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PDR A 1

Chain	Residue
A	LEU1005
A	GLY1006
A	GLN1007
A	ALA1031
A	GLU1080
A	MET1082
A	THR1083
A	GLY1085
A	MET1142

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EPE A 1287

Chain	Residue
A	ARG1177
A	GLN1211
C	GLY1228
C	ARG1246

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 3

Chain	Residue
A	LYS1088
A	ARG1092
A	ARG1095
A	ALA1209
C	ARG1246
C	GLN1250

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDR B 2

Chain	Residue
B	LEU1005
B	GLY1006
B	ALA1031
B	LYS1033
B	GLU1080
B	LEU1081
B	MET1082
B	THR1083
B	GLY1085
D	ASN1252

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1287

Chain	Residue
B	ARG1177
B	GLN1211
D	LEU1230

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PDR C 3

Chain	Residue
C	LEU1005
C	GLY1006
C	VAL1013
C	ALA1031
C	GLU1080
C	MET1082
C	THR1083
C	GLY1085
C	MET1142

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PDR D 4

Chain	Residue
D	LEU1005
D	GLY1006
D	MET1079
D	GLU1080
D	MET1082
D	THR1083
D	GLY1085
D	MET1142

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU1005-LYS1033

---

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

Chain	Residue	Details
A	PHE1131-VAL1143

---

site_id	PS00239
Number of Residues	9
Details	RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR

Chain	Residue	Details
A	ASP1159-ARG1167

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"11694888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18501599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19041240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26584640","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by GSK3-beta","evidences":[{"source":"UniProtKB","id":"Q60751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q60751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	10
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21994939","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"11694888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18501599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19041240","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---