5KGI
Crystal structure of PIM1 with inhibitor 2-[3,4-bis(chloranyl)phenoxy]ethanamine
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | ILE133 |
| A | ASP170 |
| A | ASP234 |
| A | GLY238 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | TRP269 |
| A | SER276 |
| A | ASP277 |
| A | ARG278 |
| A | GLU283 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG136 |
| A | ALA138 |
| A | LEU139 |
| A | GLN140 |
| A | LEU143 |
| A | HOH523 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ARG221 |
| A | SER222 |
| A | THR280 |
| A | PHE281 |
| A | HOH503 |
| A | HOH545 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | PHE100 |
| A | GLU153 |
| A | ASN160 |
| A | GLN264 |
| A | ARG268 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLY48 |
| A | PHE49 |
| A | ASP186 |
| A | GLY188 |
| A | SER189 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASP114 |
| A | LEU193 |
| A | HOH536 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ASP170 |
| A | GLU171 |
| A | TYR207 |
| A | ILE240 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | LYS67 |
| A | ASP186 |
| A | 6SF414 |
| A | HOH501 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | GLU262 |
| A | HIS265 |
| A | HIS287 |
| A | PRO288 |
| A | EDO411 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | TRP269 |
| A | GLU283 |
| A | ASN286 |
| A | HIS287 |
| A | PRO288 |
| A | EDO410 |
| A | HOH539 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 412 |
| Chain | Residue |
| A | TYR53 |
| A | LEU193 |
| A | LYS194 |
| A | GLY220 |
| A | ARG221 |
| A | HOH505 |
| A | HOH528 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 413 |
| Chain | Residue |
| A | GLU141 |
| A | GLU142 |
| A | HOH573 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue 6SF A 414 |
| Chain | Residue |
| A | PHE49 |
| A | ALA65 |
| A | GLU121 |
| A | LEU174 |
| A | EDO409 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 415 |
| Chain | Residue |
| A | ARG156 |
| A | ARG258 |
| A | SER261 |
| A | PHE281 |
| A | HOH502 |
| A | HOH532 |
| A | HOH545 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 416 |
| Chain | Residue |
| A | ASP108 |
| A | TRP109 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK |
| Chain | Residue | Details |
| A | LEU44-LYS67 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI |
| Chain | Residue | Details |
| A | VAL163-ILE175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 252 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15525646","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15808862","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






