9GP1
Jumonji domain-containing protein 2A with crystallization epitope mutatios K330R:A334E
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698 |
Chain | Residue | Details |
A | TYR133 | |
D | TYR133 | |
D | ASN199 | |
D | LYS207 | |
A | ASN199 | |
A | LYS207 | |
B | TYR133 | |
B | ASN199 | |
B | LYS207 | |
C | TYR133 | |
C | ASN199 | |
C | LYS207 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
A | HIS189 | |
A | HIS277 | |
B | HIS189 | |
B | HIS277 | |
C | HIS189 | |
C | HIS277 | |
D | HIS189 | |
D | HIS277 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 |
Chain | Residue | Details |
A | GLU191 | |
B | GLU191 | |
C | GLU191 | |
D | GLU191 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
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 | CYS235 | |
C | HIS241 | |
C | CYS307 | |
C | CYS309 | |
D | CYS235 | |
D | HIS241 | |
D | CYS307 | |
D | CYS309 | |
A | HIS241 | |
A | CYS307 | |
A | CYS309 | |
B | CYS235 | |
B | HIS241 | |
B | CYS307 | |
B | CYS309 | |
C | CYS235 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:B2RXH2 |
Chain | Residue | Details |
A | LYS242 | |
B | LYS242 | |
C | LYS242 | |
D | LYS242 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA3 | |
B | ALA3 | |
C | ALA3 | |
D | ALA4 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
A | GLY171 | hydrogen bond acceptor, steric role |
A | TYR178 | hydrogen bond donor, steric role |
A | HIS189 | metal ligand |
A | GLU191 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
A | HIS277 | metal ligand |
A | SER289 | hydrogen bond donor, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
B | GLY171 | hydrogen bond acceptor, steric role |
B | TYR178 | hydrogen bond donor, steric role |
B | HIS189 | metal ligand |
B | GLU191 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
B | HIS277 | metal ligand |
B | SER289 | hydrogen bond donor, steric role |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
C | GLY171 | hydrogen bond acceptor, steric role |
C | TYR178 | hydrogen bond donor, steric role |
C | HIS189 | metal ligand |
C | GLU191 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
C | HIS277 | metal ligand |
C | SER289 | hydrogen bond donor, steric role |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 370 |
Chain | Residue | Details |
D | GLY171 | hydrogen bond acceptor, steric role |
D | TYR178 | hydrogen bond donor, steric role |
D | HIS189 | metal ligand |
D | GLU191 | attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, steric role |
D | HIS277 | metal ligand |
D | SER289 | hydrogen bond donor, steric role |