2VD7
Crystal Structure of JMJD2A complexed with inhibitor Pyridine-2,4- dicarboxylic acid
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI A 501 |
Chain | Residue |
A | HIS188 |
A | GLU190 |
A | HIS276 |
A | PD21356 |
A | HOH2096 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | CYS234 |
A | HIS240 |
A | CYS306 |
A | CYS308 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI B 501 |
Chain | Residue |
B | HIS188 |
B | GLU190 |
B | HIS276 |
B | PD21356 |
B | HOH2100 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | CYS234 |
B | HIS240 |
B | CYS306 |
B | CYS308 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PD2 A 1356 |
Chain | Residue |
A | TYR132 |
A | TYR177 |
A | PHE185 |
A | HIS188 |
A | GLU190 |
A | LYS206 |
A | TRP208 |
A | LYS241 |
A | HIS276 |
A | NI501 |
A | HOH2091 |
A | HOH2096 |
A | HOH2121 |
A | HOH2172 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PD2 B 1356 |
Chain | Residue |
B | TYR132 |
B | TYR177 |
B | PHE185 |
B | HIS188 |
B | GLU190 |
B | LYS206 |
B | TRP208 |
B | LYS241 |
B | HIS276 |
B | NI501 |
B | HOH2091 |
B | HOH2100 |
B | HOH2132 |
B | HOH2184 |
B | HOH2185 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698 |
Chain | Residue | Details |
A | TYR132 | |
A | ASN198 | |
A | LYS206 | |
B | TYR132 | |
B | ASN198 | |
B | LYS206 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
A | HIS188 | |
A | HIS276 | |
B | HIS188 | |
B | HIS276 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
A | GLU190 | |
B | GLU190 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I |
Chain | Residue | Details |
A | CYS234 | |
A | HIS240 | |
A | CYS306 | |
A | CYS308 | |
B | CYS234 | |
B | HIS240 | |
B | CYS306 | |
B | CYS308 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:B2RXH2 |
Chain | Residue | Details |
A | LYS241 | |
B | LYS241 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
A | GLY170 | hydrogen bond acceptor, steric role |
A | TYR177 | hydrogen bond donor, steric role |
A | HIS188 | metal ligand |
A | GLU190 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
A | HIS276 | metal ligand |
A | SER288 | hydrogen bond donor, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
B | GLY170 | hydrogen bond acceptor, steric role |
B | TYR177 | hydrogen bond donor, steric role |
B | HIS188 | metal ligand |
B | GLU190 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
B | HIS276 | metal ligand |
B | SER288 | hydrogen bond donor, steric role |