7BVJ
UDP-N-acetylglucosamine 3-dehydrogenase GnnA from Acidithiobacillus ferrooxidans (P21)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
A | 0009245 | biological_process | lipid A biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
B | 0009245 | biological_process | lipid A biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
C | 0009245 | biological_process | lipid A biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
D | 0009245 | biological_process | lipid A biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY12 |
A | HOH553 |
A | HOH610 |
A | HOH627 |
A | HIS13 |
A | LEU14 |
A | ASP33 |
A | GLU34 |
A | ARG38 |
A | THR68 |
A | PRO69 |
A | HOH531 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue F8U A 402 |
Chain | Residue |
A | ARG223 |
A | TYR230 |
A | SER232 |
A | HOH507 |
A | HOH516 |
B | VAL215 |
B | ARG216 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | GLY12 |
B | HIS13 |
B | LEU14 |
B | ASP33 |
B | GLU34 |
B | ARG38 |
B | THR68 |
B | PRO69 |
B | HOH534 |
B | HOH609 |
B | HOH612 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | GLY12 |
C | HIS13 |
C | LEU14 |
C | ASP33 |
C | GLU34 |
C | ARG38 |
C | THR68 |
C | PRO69 |
C | ARG151 |
C | HOH504 |
C | HOH509 |
C | HOH515 |
C | HOH582 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue NAD D 401 |
Chain | Residue |
D | GLY12 |
D | HIS13 |
D | LEU14 |
D | ASP33 |
D | GLU34 |
D | ARG38 |
D | THR68 |
D | PRO69 |
D | HOH537 |
D | HOH574 |
D | HOH612 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33200610, ECO:0007744|PDB:7BVJ |
Chain | Residue | Details |
A | HIS13 | |
A | LEU14 | |
B | HIS13 | |
B | LEU14 | |
C | HIS13 | |
C | LEU14 | |
D | HIS13 | |
D | LEU14 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33200610, ECO:0007744|PDB:7BVJ, ECO:0007744|PDB:7BVK |
Chain | Residue | Details |
A | ARG38 | |
B | ARG38 | |
C | ARG38 | |
D | ARG38 |