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 | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016 |
| Chain | Residue | Details |
| B | ASP1132 | |
| D | ASP1132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 |
| Chain | Residue | Details |
| B | SER1006 | |
| D | ASP1150 | |
| B | LYS1030 | |
| B | GLU1077 | |
| B | ARG1136 | |
| B | ASP1150 | |
| D | SER1006 | |
| D | LYS1030 | |
| D | GLU1077 | |
| D | ARG1136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
| Chain | Residue | Details |
| B | TYR984 | |
| D | TYR984 | |
| C | ALA215 | |
| C | GLN262 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462 |
| Chain | Residue | Details |
| B | CYS1056 | |
| D | CYS1056 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 |
| Chain | Residue | Details |
| B | PTR1158 | |
| B | PTR1162 | |
| B | PTR1163 | |
| D | PTR1158 | |
| D | PTR1162 | |
| D | PTR1163 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER50 | |
| C | SER50 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745 |
| Chain | Residue | Details |
| A | TYR66 | |
| C | TYR66 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477 |
| Chain | Residue | Details |
| A | ALA215 | |
| C | ALA215 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872 |
| Chain | Residue | Details |
| A | SER242 | |
| A | SER243 | |
| C | SER242 | |
| C | SER243 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CROSSLNK: N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339 |
| Chain | Residue | Details |
| A | ALA215 | |
| A | SER216 | |
| C | ALA215 | |
| C | SER216 |
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 |
