5A7W
Crystal structure of human JMJD2A in complex with compound 35
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1354 |
Chain | Residue |
A | PHE227 |
A | PRO228 |
A | GLY229 |
A | SER230 |
B | LYS105 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1354 |
Chain | Residue |
B | SER230 |
A | LYS105 |
B | PHE227 |
B | PRO228 |
B | GLY229 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 35M B 1355 |
Chain | Residue |
B | ASN86 |
B | TYR132 |
B | ASP135 |
B | TYR177 |
B | PHE185 |
B | HIS188 |
B | GLU190 |
B | ASN198 |
B | LYS206 |
B | TRP208 |
B | LYS241 |
B | MN1356 |
B | DMS1361 |
B | HOH2013 |
B | HOH2022 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 35M A 1355 |
Chain | Residue |
A | ASN86 |
A | TYR132 |
A | PHE185 |
A | HIS188 |
A | GLU190 |
A | ASN198 |
A | LYS206 |
A | TRP208 |
A | LYS241 |
A | MN1356 |
A | DMS1360 |
A | HOH2007 |
A | HOH2011 |
A | HOH2019 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 1356 |
Chain | Residue |
A | HIS188 |
A | GLU190 |
A | HIS276 |
A | 35M1355 |
A | HOH2019 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 1356 |
Chain | Residue |
B | HIS188 |
B | GLU190 |
B | HIS276 |
B | 35M1355 |
B | HOH2022 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1357 |
Chain | Residue |
A | CYS234 |
A | HIS240 |
A | CYS306 |
A | CYS308 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1357 |
Chain | Residue |
B | CYS234 |
B | HIS240 |
B | CYS306 |
B | CYS308 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1358 |
Chain | Residue |
B | LYS224 |
B | ALA236 |
B | PHE237 |
B | LEU238 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 1359 |
Chain | Residue |
B | PHE114 |
B | THR261 |
B | HIS281 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1360 |
Chain | Residue |
B | THR83 |
B | PHE227 |
B | SER230 |
B | HIS240 |
B | THR243 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 1358 |
Chain | Residue |
A | LYS90 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1359 |
Chain | Residue |
A | GLU235 |
A | ALA236 |
A | PHE237 |
A | LEU238 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS B 1361 |
Chain | Residue |
B | GLY170 |
B | TYR175 |
B | TYR177 |
B | GLU190 |
B | SER288 |
B | ASN290 |
B | 35M1355 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 1360 |
Chain | Residue |
A | GLY170 |
A | TYR175 |
A | TYR177 |
A | SER288 |
A | 35M1355 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698 |
Chain | Residue | Details |
B | TYR132 | |
B | ASN198 | |
B | LYS206 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
B | HIS188 | |
B | HIS276 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
B | GLU190 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 |
B | CYS234 | |
B | HIS240 | |
B | CYS306 | |
B | CYS308 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:B2RXH2 |
Chain | Residue | Details |
B | LYS241 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
B | ALA2 |
Catalytic Information from CSA
site_id | MCSA1 |
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 |