3PUQ
CEKDM7A from C.Elegans, complex with alpha-KG
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 | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20567261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21251613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21251613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
