Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2B4S

Crystal structure of a complex between PTP1B and the insulin receptor tyrosine kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0016311	biological_process	dephosphorylation
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	0004725	molecular_function	protein tyrosine phosphatase activity
C	0006470	biological_process	protein dephosphorylation
C	0016311	biological_process	dephosphorylation
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	10
Details	BINDING SITE FOR RESIDUE SO4 A 1000

Chain	Residue
A	ALA215
A	HOH1042
A	SER216
A	ALA217
A	GLY218
A	ILE219
A	GLY220
A	ARG221
A	SER222
A	HOH1016

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1001

Chain	Residue
A	TYR20
A	ARG24
A	ARG254
A	GLY259
A	HOH1015

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 C 1002

Chain	Residue
C	ALA215
C	SER216
C	ALA217
C	GLY218
C	ILE219
C	GLY220
C	ARG221
C	SER222
C	HOH1030
C	HOH1058

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1003

Chain	Residue
C	TYR20
C	ARG24
C	ARG254
C	GLY259
C	HOH1037

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1004

Chain	Residue
A	ASN111
A	ARG112
A	LEU119
A	LYS120
A	ASP181
A	SER216
A	ARG221
A	HOH1094
B	HOH208

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 C 1005

Chain	Residue
C	ASN111
C	ARG112
C	LEU119
C	LYS120
C	ASP181
C	SER216
C	ARG221
C	HOH1061
D	HOH231
D	GLU1273

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1284

Chain	Residue
B	PRO1235
B	GLU1236
D	HOH211
D	PRO1235
D	GLU1236
D	ARG1237

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1007

Chain	Residue
A	ASN42
A	ARG43
A	ASN90

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1008

Chain	Residue
A	ARG45
A	CYS121
A	ALA122

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 1009

Chain	Residue
B	ASN1249
B	ASN1251
C	ARG45
C	PRO89
C	CYS121
C	ALA122

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU1002-LYS1030

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

Chain	Residue	Details
B	PHE1128-VAL1140

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

Chain	Residue	Details
B	ASP1156-ARG1164

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Phosphocysteine intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKB/AKT1, CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11579209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"9355745","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"PubMed","id":"22169477","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form","evidences":[{"source":"PubMed","id":"12802338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12802339","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"38056462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26584640","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"27577745","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG221
A	ASP181
A	ALA215
A	SER222

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ARG221
C	ASP181
C	ALA215
C	SER222

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

Chain	Residue	Details
B	ASP1132
B	ARG1136

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

Chain	Residue	Details
D	ASP1132
D	ARG1136

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP1132
B	ALA1134

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP1132
D	ALA1134

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP1132
B	ASN1137
B	ALA1134

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP1132
D	ASN1137
D	ALA1134

site_id	MCSA1
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
B	ASP1132	increase nucleophilicity, proton acceptor, proton donor, steric role
B	ARG1136	electrostatic stabiliser, increase electrophilicity, promote heterolysis
B	ASN1137	metal ligand
B	ASP1150	metal ligand
A	GLN262	steric role

site_id	MCSA2
Number of Residues	4
Details	M-CSA 246

Chain	Residue	Details
D	ASP1132	increase nucleophilicity, proton acceptor, proton donor, steric role
D	ARG1136	electrostatic stabiliser, increase electrophilicity, promote heterolysis
D	ASN1137	metal ligand
D	ASP1150	metal ligand
C	GLN262	steric role

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)