3U4S
Histone Lysine demethylase JMJD2A in complex with T11C peptide substrate crosslinked to N-oxalyl-D-cysteine
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 | 08P503 |
A | HOH719 |
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 | 14 |
Details | BINDING SITE FOR RESIDUE 08P A 503 |
Chain | Residue |
A | TYR132 |
A | TYR177 |
A | PHE185 |
A | HIS188 |
A | GLU190 |
A | SER196 |
A | ASN198 |
A | LYS206 |
A | TRP208 |
A | HIS276 |
A | SER288 |
A | NI501 |
C | M3L9 |
C | CYS11 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI B 501 |
Chain | Residue |
B | HIS188 |
B | GLU190 |
B | HIS276 |
B | 08P503 |
B | HOH752 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | CYS234 |
B | HIS240 |
B | CYS306 |
B | CYS308 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 08P B 503 |
Chain | Residue |
B | TYR132 |
B | TYR177 |
B | PHE185 |
B | HIS188 |
B | GLU190 |
B | SER196 |
B | ASN198 |
B | LYS206 |
B | HIS276 |
B | SER288 |
B | NI501 |
B | HOH752 |
D | M3L9 |
D | CYS11 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 |
Chain | Residue | Details |
C | ARG8 | |
D | ARG8 | |
A | LYS206 | |
B | TYR132 | |
B | ASN198 | |
B | LYS206 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
C | M3L9 | |
D | M3L9 | |
B | HIS188 | |
B | HIS276 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 |
Chain | Residue | Details |
C | SER10 | |
D | SER10 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 |
Chain | Residue | Details |
C | CYS11 | |
D | CYS11 | |
A | CYS306 | |
A | CYS308 | |
B | CYS234 | |
B | HIS240 | |
B | CYS306 | |
B | CYS308 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
C | LYS14 | |
D | LYS14 |
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 |