3G2F
Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| A | 0016020 | cellular_component | membrane |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP A 900 |
| Chain | Residue |
| A | HOH62 |
| A | GLY212 |
| A | ARG213 |
| A | TYR214 |
| A | GLY215 |
| A | VAL217 |
| A | ALA228 |
| A | LYS230 |
| A | MET279 |
| A | GLU280 |
| A | TYR282 |
| A | HOH71 |
| A | SER286 |
| A | ARG337 |
| A | ASN338 |
| A | LEU340 |
| A | ASP351 |
| A | MG901 |
| A | HOH73 |
| A | HOH74 |
| A | HOH75 |
| A | HOH119 |
| A | ILE209 |
| A | GLY210 |
| A | ARG211 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | HOH76 |
| A | HOH119 |
| A | ASN338 |
| A | ASP351 |
| A | ADP900 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | HOH78 |
| A | HOH79 |
| A | ARG337 |
| A | ARG381 |
| A | ASN442 |
| A | HIS443 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 3 |
| Chain | Residue |
| A | GLN458 |
| A | ARG459 |
| A | PRO460 |
| A | LYS461 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 4 |
| Chain | Residue |
| A | ASN256 |
| A | HIS306 |
| A | SER307 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | HOH42 |
| A | HOH105 |
| A | ASN393 |
| A | ALA400 |
| A | GLN403 |
| A | ALA488 |
| A | GLU489 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP B 900 |
| Chain | Residue |
| B | ILE209 |
| B | GLY210 |
| B | GLY212 |
| B | ARG213 |
| B | TYR214 |
| B | GLY215 |
| B | VAL217 |
| B | ALA228 |
| B | LYS230 |
| B | MET279 |
| B | GLU280 |
| B | TYR282 |
| B | SER286 |
| B | ARG337 |
| B | ASN338 |
| B | LEU340 |
| B | ASP351 |
| B | MG901 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | ASN338 |
| B | ASP351 |
| B | ADP900 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1 |
| Chain | Residue |
| B | ARG211 |
| B | ARG337 |
| B | ARG381 |
| B | ASN442 |
| B | HIS443 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 6 |
| Chain | Residue |
| B | HOH116 |
| B | ARG459 |
| B | PRO460 |
| B | LYS461 |
| B | PHE462 |
| B | TRP484 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 22 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGRYGAVYkGslderp............VAVK |
| Chain | Residue | Details |
| A | ILE209-LYS230 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of the BMPR2 kinase domain.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ARG337 | |
| A | ASP333 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ARG337 | |
| B | ASP333 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN335 | |
| A | ASP333 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN335 | |
| B | ASP333 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN338 | |
| A | ASN335 | |
| A | ASP333 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN338 | |
| B | ASN335 | |
| B | ASP333 |
