5AHS
3-Sulfinopropionyl-Coenzyme A (3SP-CoA) desulfinase from Advenella mimgardefordensis DPN7T: holo crystal structure with the substrate analog succinyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD A 410 |
| Chain | Residue |
| A | ILE121 |
| A | MET361 |
| A | ILE364 |
| A | ALA365 |
| A | GLY366 |
| A | THR368 |
| A | GLN370 |
| A | ILE371 |
| A | GLN387 |
| A | COA411 |
| A | HOH2115 |
| A | ILE123 |
| A | HOH2148 |
| A | HOH2155 |
| A | HOH2326 |
| B | ARG272 |
| B | GLN274 |
| B | PHE275 |
| B | LEU279 |
| B | PHE282 |
| B | GLN283 |
| B | LEU285 |
| A | SER124 |
| B | TRP287 |
| B | GLN339 |
| B | PHE340 |
| B | GLY342 |
| B | SER343 |
| A | GLY129 |
| A | SER130 |
| A | TYR153 |
| A | TRP154 |
| A | THR156 |
| A | GLU210 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE COA A 411 |
| Chain | Residue |
| A | SER124 |
| A | GLY129 |
| A | SER130 |
| A | ALA237 |
| A | MET240 |
| A | SER241 |
| A | TYR243 |
| A | ASN244 |
| A | ARG247 |
| A | ILE316 |
| A | GLY366 |
| A | ILE371 |
| A | LYS384 |
| A | FAD410 |
| A | HOH2225 |
| A | HOH2305 |
| A | HOH2319 |
| A | HOH2321 |
| A | HOH2327 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B 410 |
| Chain | Residue |
| A | ARG272 |
| A | GLN274 |
| A | PHE275 |
| A | LEU279 |
| A | PHE282 |
| A | GLN283 |
| A | LEU285 |
| A | TRP287 |
| A | GLN339 |
| A | PHE340 |
| A | GLY342 |
| A | SER343 |
| A | HOH2235 |
| B | ILE121 |
| B | ILE123 |
| B | SER124 |
| B | GLY129 |
| B | SER130 |
| B | TYR153 |
| B | TRP154 |
| B | THR156 |
| B | GLU210 |
| B | MET361 |
| B | GLY366 |
| B | THR368 |
| B | GLN370 |
| B | ILE371 |
| B | GLN387 |
| B | COA411 |
| B | HOH2131 |
| B | HOH2137 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE COA B 411 |
| Chain | Residue |
| B | SER124 |
| B | SER130 |
| B | ALA237 |
| B | MET240 |
| B | SER241 |
| B | TYR243 |
| B | ASN244 |
| B | ARG247 |
| B | ILE316 |
| B | GLY366 |
| B | ILE371 |
| B | LYS384 |
| B | FAD410 |
| B | HOH2255 |
| B | HOH2263 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD C 410 |
| Chain | Residue |
| C | ILE121 |
| C | ILE123 |
| C | SER124 |
| C | GLY129 |
| C | SER130 |
| C | TYR153 |
| C | TRP154 |
| C | THR156 |
| C | GLU210 |
| C | MET361 |
| C | ILE364 |
| C | ALA365 |
| C | GLY366 |
| C | GLY367 |
| C | THR368 |
| C | GLN370 |
| C | ILE371 |
| C | GLN387 |
| C | HOH2085 |
| C | HOH2088 |
| C | HOH2094 |
| C | HOH2235 |
| E | ARG272 |
| E | GLN274 |
| E | PHE275 |
| E | LEU279 |
| E | PHE282 |
| E | LEU285 |
| E | GLN339 |
| E | PHE340 |
| E | GLY342 |
| E | SER343 |
| F | GLN283 |
| F | TRP287 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SIN C 412 |
| Chain | Residue |
| C | ARG84 |
| C | VAL87 |
| C | ASP88 |
| C | GLN246 |
| C | ALA250 |
| C | VAL253 |
| C | PHE362 |
| C | ALA365 |
| C | GLY366 |
| C | HOH2065 |
| C | HOH2150 |
| C | HOH2188 |
| site_id | AC7 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD D 410 |
| Chain | Residue |
| D | ILE121 |
| D | ILE123 |
| D | SER124 |
| D | GLY129 |
| D | SER130 |
| D | TYR153 |
| D | TRP154 |
| D | THR156 |
| D | GLU210 |
| D | MET361 |
| D | ILE364 |
| D | ALA365 |
| D | GLY366 |
| D | THR368 |
| D | GLN370 |
| D | ILE371 |
| D | GLN387 |
| D | COA411 |
| D | HOH2091 |
| D | HOH2099 |
| E | GLN283 |
| E | TRP287 |
| F | ARG272 |
| F | GLN274 |
| F | PHE275 |
| F | LEU279 |
| F | PHE282 |
| F | LEU285 |
| F | GLN339 |
| F | PHE340 |
| F | GLY342 |
| F | SER343 |
| F | HOH2122 |
| F | HOH2170 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA D 411 |
| Chain | Residue |
| D | SER124 |
| D | SER130 |
| D | SER133 |
| D | ALA237 |
| D | MET240 |
| D | SER241 |
| D | TYR243 |
| D | ASN244 |
| D | ARG247 |
| D | ILE316 |
| D | GLY366 |
| D | ILE371 |
| D | LYS384 |
| D | FAD410 |
| D | HOH2092 |
| D | HOH2150 |
| D | HOH2212 |
| D | HOH2220 |
| site_id | AC9 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD E 410 |
| Chain | Residue |
| C | ARG272 |
| C | GLN274 |
| C | PHE275 |
| C | LEU279 |
| C | PHE282 |
| C | LEU285 |
| C | GLN339 |
| C | PHE340 |
| C | SER343 |
| C | HOH2159 |
| C | HOH2201 |
| D | GLN283 |
| D | TRP287 |
| E | ARG84 |
| E | ILE121 |
| E | ILE123 |
| E | SER124 |
| E | GLY129 |
| E | SER130 |
| E | TYR153 |
| E | TRP154 |
| E | THR156 |
| E | GLU210 |
| E | MET361 |
| E | ALA365 |
| E | GLY366 |
| E | GLY367 |
| E | THR368 |
| E | GLN370 |
| E | ILE371 |
| E | GLN387 |
| E | COA411 |
| E | HOH2067 |
| E | HOH2068 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE COA E 411 |
| Chain | Residue |
| E | SER124 |
| E | SER130 |
| E | SER133 |
| E | ALA237 |
| E | MET240 |
| E | SER241 |
| E | TYR243 |
| E | ASN244 |
| E | ARG247 |
| E | ILE316 |
| E | GLY366 |
| E | GLY367 |
| E | ILE371 |
| E | LYS384 |
| E | FAD410 |
| E | HOH2196 |
| site_id | BC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD F 410 |
| Chain | Residue |
| C | GLN283 |
| C | TRP287 |
| D | ARG272 |
| D | GLN274 |
| D | PHE275 |
| D | LEU279 |
| D | PHE282 |
| D | LEU285 |
| D | GLN339 |
| D | PHE340 |
| D | GLY342 |
| D | SER343 |
| F | ARG84 |
| F | ILE121 |
| F | ILE123 |
| F | SER124 |
| F | GLY129 |
| F | SER130 |
| F | TYR153 |
| F | TRP154 |
| F | THR156 |
| F | GLU210 |
| F | MET361 |
| F | ILE364 |
| F | GLY366 |
| F | THR368 |
| F | GLN370 |
| F | ILE371 |
| F | GLN387 |
| F | COA411 |
| F | HOH2057 |
| F | HOH2085 |
| F | HOH2192 |
| site_id | BC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE COA F 411 |
| Chain | Residue |
| F | SER124 |
| F | SER130 |
| F | SER133 |
| F | ALA237 |
| F | MET240 |
| F | SER241 |
| F | TYR243 |
| F | ASN244 |
| F | ARG247 |
| F | ILE316 |
| F | GLY366 |
| F | ILE371 |
| F | FAD410 |
| F | HOH2109 |
| F | HOH2186 |
| F | HOH2193 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1393 |
| Chain | Residue |
| B | HOH2051 |
| B | HOH2066 |
| C | GLU34 |
| E | ARG348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26057676, ECO:0007744|PDB:5AF7, ECO:0007744|PDB:5AHS |
| Chain | Residue | Details |
| A | ILE121 | |
| B | SER130 | |
| B | TYR153 | |
| B | ARG272 | |
| B | GLN339 | |
| B | SER343 | |
| B | GLY366 | |
| B | GLN387 | |
| C | ILE121 | |
| C | SER130 | |
| C | TYR153 | |
| A | SER130 | |
| C | ARG272 | |
| C | GLN339 | |
| C | SER343 | |
| C | GLY366 | |
| C | GLN387 | |
| D | ILE121 | |
| D | SER130 | |
| D | TYR153 | |
| D | ARG272 | |
| D | GLN339 | |
| A | TYR153 | |
| D | SER343 | |
| D | GLY366 | |
| D | GLN387 | |
| E | ILE121 | |
| E | SER130 | |
| E | TYR153 | |
| E | ARG272 | |
| E | GLN339 | |
| E | SER343 | |
| E | GLY366 | |
| A | ARG272 | |
| E | GLN387 | |
| F | ILE121 | |
| F | SER130 | |
| F | TYR153 | |
| F | ARG272 | |
| F | GLN339 | |
| F | SER343 | |
| F | GLY366 | |
| F | GLN387 | |
| A | GLN339 | |
| A | SER343 | |
| A | GLY366 | |
| A | GLN387 | |
| B | ILE121 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:26057676 |
| Chain | Residue | Details |
| A | TYR243 | |
| B | TYR243 | |
| C | TYR243 | |
| D | TYR243 | |
| E | TYR243 | |
| F | TYR243 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | SITE: Important for activity => ECO:0000269|PubMed:26057676 |
| Chain | Residue | Details |
| A | ARG84 | |
| B | ARG84 | |
| C | ARG84 | |
| D | ARG84 | |
| E | ARG84 | |
| F | ARG84 |
