8RFM
Human NOQ1 enzyme in complex with NADH by serial crystallography
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 |
Chain | Residue | Details |
A | HIS12 | |
B | GLN67 | |
B | LEU104 | |
B | THR148 | |
B | TYR156 | |
B | ARG201 | |
C | HIS12 | |
C | PHE18 | |
C | GLN67 | |
C | LEU104 | |
C | THR148 | |
A | PHE18 | |
C | TYR156 | |
C | ARG201 | |
D | HIS12 | |
D | PHE18 | |
D | GLN67 | |
D | LEU104 | |
D | THR148 | |
D | TYR156 | |
D | ARG201 | |
A | GLN67 | |
A | LEU104 | |
A | THR148 | |
A | TYR156 | |
A | ARG201 | |
B | HIS12 | |
B | PHE18 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ALA126 | |
B | ALA126 | |
C | ALA126 | |
D | ALA126 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER82 | |
B | SER82 | |
C | SER82 | |
D | SER82 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS250 | |
D | LYS250 | |
D | LYS251 | |
A | LYS251 | |
B | LYS250 | |
B | LYS251 | |
C | LYS250 | |
C | LYS251 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 3 |
Chain | Residue | Details |
A | GLY150 | electrostatic stabiliser, hydrogen bond donor |
A | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 3 |
Chain | Residue | Details |
B | GLY150 | electrostatic stabiliser, hydrogen bond donor |
B | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 3 |
Chain | Residue | Details |
C | GLY150 | electrostatic stabiliser, hydrogen bond donor |
C | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 3 |
Chain | Residue | Details |
D | GLY150 | electrostatic stabiliser, hydrogen bond donor |
D | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |