3KV4
Structure of PHF8 in complex with histone H3
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 448 |
Chain | Residue |
A | CYS8 |
A | CYS10 |
A | HIS31 |
A | CYS34 |
A | EDO452 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 449 |
Chain | Residue |
A | CYS23 |
A | CYS26 |
A | CYS50 |
A | CYS53 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 A 450 |
Chain | Residue |
A | HIS247 |
A | ASP249 |
A | HIS319 |
A | HOH553 |
A | OGA5798 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI A 451 |
Chain | Residue |
A | SER214 |
A | TRP215 |
A | VAL216 |
A | PHE334 |
A | LEU335 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE EDO A 452 |
Chain | Residue |
A | CYS10 |
A | LEU12 |
A | ARG18 |
A | HIS31 |
A | CYS34 |
A | LEU104 |
A | PHE115 |
A | GLU118 |
A | ASN119 |
A | ZN448 |
A | HOH472 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 453 |
Chain | Residue |
A | ARG92 |
A | ASN202 |
A | ILE265 |
A | LYS302 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 454 |
Chain | Residue |
A | PHE96 |
A | SER98 |
A | ARG199 |
A | HOH500 |
A | HOH512 |
A | HOH608 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 455 |
Chain | Residue |
A | ARG270 |
A | HOH514 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 456 |
Chain | Residue |
A | ARG18 |
A | SER33 |
A | GLU118 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 457 |
Chain | Residue |
A | LYS212 |
A | LEU213 |
A | SER214 |
A | TRP215 |
A | EDO459 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 458 |
Chain | Residue |
A | ARG89 |
A | ASP131 |
A | GLY132 |
A | GLY134 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 459 |
Chain | Residue |
A | SER337 |
A | HIS374 |
A | ILE378 |
A | EDO457 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 460 |
Chain | Residue |
A | ASP44 |
A | ILE45 |
A | SER60 |
A | ILE61 |
A | MET62 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 461 |
Chain | Residue |
A | VAL35 |
A | VAL37 |
A | TYR48 |
A | HIS49 |
A | PRO51 |
A | GLU54 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 462 |
Chain | Residue |
A | ASN52 |
A | VAL55 |
A | SER98 |
A | ASP100 |
A | GLU101 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 463 |
Chain | Residue |
A | THR355 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 464 |
Chain | Residue |
A | ASP161 |
A | CYS168 |
A | MET170 |
A | LYS186 |
site_id | BC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE OGA A 5798 |
Chain | Residue |
A | ASN189 |
A | THR244 |
A | HIS247 |
A | ASP249 |
A | TYR257 |
A | LYS264 |
A | HIS319 |
A | VAL321 |
A | FE2450 |
A | HOH479 |
A | HOH553 |
B | MLY9 |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
B | LYS14-LEU20 |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. ClCrlPYdvtrfmieC |
Chain | Residue | Details |
A | CYS8-CYS23 |
site_id | PS01359 |
Number of Residues | 46 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. Cl.Crlpydvtrfm...................................IeCdm..Cqdw.FHgsCvgveeekaadidl................................YhCpnC |
Chain | Residue | Details |
A | CYS8-CYS53 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 156 |
Details | Domain: {"description":"JmjC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 51 |
Details | Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20023638","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20101266","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"20622854","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"20622854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |