7EJI
Crystal structure of KRED F147L/L153Q/Y190P/L199A/M205F/M206F variant and methyl methacrylate complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SieglvgdptQgaYNASKGAVrIMSkSAA |
Chain | Residue | Details |
A | SER143-ALA171 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:26644568 |
Chain | Residue | Details |
A | TYR156 | |
B | TYR156 | |
C | TYR156 | |
D | TYR156 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF2 |
Chain | Residue | Details |
A | THR16 | |
B | ASP63 | |
B | ASN90 | |
B | TYR156 | |
B | LYS160 | |
B | ILE191 | |
C | THR16 | |
C | ARG39 | |
C | ASP63 | |
C | ASN90 | |
C | TYR156 | |
A | ARG39 | |
C | LYS160 | |
C | ILE191 | |
D | THR16 | |
D | ARG39 | |
D | ASP63 | |
D | ASN90 | |
D | TYR156 | |
D | LYS160 | |
D | ILE191 | |
A | ASP63 | |
A | ASN90 | |
A | TYR156 | |
A | LYS160 | |
A | ILE191 | |
B | THR16 | |
B | ARG39 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26644568, ECO:0007744|PDB:4RF4 |
Chain | Residue | Details |
A | GLN252 | |
B | GLN252 | |
C | GLN252 | |
D | GLN252 |