4GD4
Crystal Structure of JMJD2A Complexed with Inhibitor
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 | 0WS504 |
A | HOH739 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE CL A 503 |
Chain | Residue |
A | GLU235 |
A | ALA236 |
A | PHE237 |
A | LEU238 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 0WS A 504 |
Chain | Residue |
A | TYR132 |
A | TYR177 |
A | PHE185 |
A | HIS188 |
A | GLU190 |
A | LYS206 |
A | TRP208 |
A | LYS241 |
A | HIS276 |
A | NI501 |
A | HOH642 |
A | HOH739 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI B 501 |
Chain | Residue |
B | HIS188 |
B | GLU190 |
B | HIS276 |
B | 0WS506 |
B | HOH728 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | CYS234 |
B | HIS240 |
B | CYS306 |
B | CYS308 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 503 |
Chain | Residue |
B | ARG98 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 504 |
Chain | Residue |
B | GLU113 |
B | GLU116 |
B | ARG119 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 505 |
Chain | Residue |
B | PHE237 |
B | LYS241 |
B | MET242 |
B | THR243 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 0WS B 506 |
Chain | Residue |
B | TYR132 |
B | TYR177 |
B | PHE185 |
B | HIS188 |
B | GLU190 |
B | LYS206 |
B | TRP208 |
B | LYS241 |
B | NI501 |
B | HOH647 |
B | HOH728 |
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 |