Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 A 1 |
Chain | Residue |
A | AKG4 |
A | HIS495 |
A | ASP497 |
A | HIS567 |
A | HOH1006 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 2 |
Chain | Residue |
A | CYS198 |
A | CYS201 |
A | HIS252 |
A | CYS255 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 3 |
Chain | Residue |
A | CYS244 |
A | CYS247 |
A | CYS271 |
A | CYS274 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AKG A 4 |
Chain | Residue |
A | FE21 |
A | ASN421 |
A | LEU423 |
A | THR492 |
A | HIS495 |
A | ASP497 |
A | TYR505 |
A | LYS512 |
A | HIS567 |
A | VAL569 |
A | HOH1006 |
A | HOH1013 |
A | HOH1111 |
A | HOH1125 |
A | HOH1629 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 5 |
Chain | Residue |
A | LEU423 |
A | ASP497 |
A | PHE498 |
A | HOH1125 |
A | HOH1713 |
A | HOH1780 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE2 C 1 |
Chain | Residue |
C | AKG4 |
C | HIS495 |
C | ASP497 |
C | HIS567 |
C | HOH1012 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 2 |
Chain | Residue |
C | CYS198 |
C | CYS201 |
C | HIS252 |
C | CYS255 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 3 |
Chain | Residue |
C | CYS244 |
C | CYS247 |
C | CYS271 |
C | CYS274 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AKG C 4 |
Chain | Residue |
C | FE21 |
C | ASN421 |
C | LEU423 |
C | THR492 |
C | HIS495 |
C | ASP497 |
C | TYR505 |
C | LYS512 |
C | HIS567 |
C | VAL569 |
C | HOH1012 |
C | HOH1023 |
C | HOH1102 |
C | HOH1140 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 5 |
Chain | Residue |
C | HIS495 |
C | ASP497 |
C | PHE498 |
C | HOH1102 |
C | HOH1443 |
Functional Information from PROSITE/UniProt
site_id | PS01359 |
Number of Residues | 77 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. CggCgkftheddlialeeekkkekekplmskkkshhhkkndfqw.....IgCds..Cqtw.YHflCsgleqfeyylyek................................FfCpkC |
Chain | Residue | Details |
A | CYS198-CYS274 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 164 |
Details | ZN_FING: PHD-type |
Chain | Residue | Details |
A | SER195-HIS277 | |
C | SER195-HIS277 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | THR492 | |
C | THR492 | |
Chain | Residue | Details |
A | HIS495 | |
A | ASP497 | |
C | HIS495 | |
C | ASP497 | |
Chain | Residue | Details |
A | TYR505 | |
A | LYS512 | |
A | HIS567 | |
C | TYR505 | |
C | LYS512 | |
C | HIS567 | |