3S2G
Crystal Structure of FurX NADH+:Furfuryl alcohol I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0008270 | molecular_function | zinc ion 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 | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0008270 | molecular_function | zinc ion 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 | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0008270 | molecular_function | zinc ion 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 | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0008270 | molecular_function | zinc ion 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| G | 0008270 | molecular_function | zinc ion binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | CYS42 |
| A | HIS65 |
| A | GLU66 |
| A | CYS152 |
| A | FU2600 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS110 |
| A | CYS96 |
| A | GLY97 |
| A | CYS99 |
| A | CYS102 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FU2 A 600 |
| Chain | Residue |
| A | CYS42 |
| A | THR44 |
| A | HIS65 |
| A | TRP91 |
| A | CYS152 |
| A | ILE289 |
| A | VAL290 |
| A | ZN500 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 701 |
| Chain | Residue |
| A | CYS42 |
| A | HIS43 |
| A | GLY179 |
| A | ARG335 |
| A | HOH399 |
| A | HOH686 |
| A | HOH989 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | ARG86 |
| A | GLY143 |
| A | PHE144 |
| A | HOH541 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | CYS42 |
| B | HIS65 |
| B | GLU66 |
| B | CYS152 |
| B | FU2600 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | CYS96 |
| B | GLY97 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FU2 B 600 |
| Chain | Residue |
| B | THR44 |
| B | HIS65 |
| B | TRP91 |
| B | CYS152 |
| B | LEU266 |
| B | ILE289 |
| B | VAL290 |
| B | ZN500 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 701 |
| Chain | Residue |
| B | CYS42 |
| B | HIS43 |
| B | GLY179 |
| B | ARG335 |
| B | HOH368 |
| B | HOH389 |
| B | HOH1143 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 702 |
| Chain | Residue |
| B | ARG86 |
| B | GLY143 |
| B | PHE144 |
| B | HOH348 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 500 |
| Chain | Residue |
| C | CYS42 |
| C | HIS65 |
| C | GLU66 |
| C | CYS152 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | CYS96 |
| C | GLY97 |
| C | CYS99 |
| C | CYS102 |
| C | CYS110 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FU2 C 600 |
| Chain | Residue |
| C | THR44 |
| C | TRP91 |
| C | LEU266 |
| C | ILE289 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 701 |
| Chain | Residue |
| C | CYS42 |
| C | HIS43 |
| C | GLY179 |
| C | ARG335 |
| C | HOH376 |
| C | HOH1160 |
| C | HOH1238 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 702 |
| Chain | Residue |
| C | ARG86 |
| C | GLY143 |
| C | PHE144 |
| C | HOH393 |
| C | HOH998 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 500 |
| Chain | Residue |
| D | CYS42 |
| D | HIS65 |
| D | GLU66 |
| D | CYS152 |
| D | FU2600 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | CYS96 |
| D | GLY97 |
| D | CYS99 |
| D | CYS102 |
| D | CYS110 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FU2 D 600 |
| Chain | Residue |
| D | THR44 |
| D | HIS65 |
| D | TRP91 |
| D | CYS152 |
| D | LEU266 |
| D | ZN500 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 701 |
| Chain | Residue |
| D | CYS42 |
| D | HIS43 |
| D | GLY179 |
| D | ARG335 |
| D | HOH373 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 702 |
| Chain | Residue |
| D | ARG86 |
| D | GLY143 |
| D | PHE144 |
| D | HOH379 |
| D | HOH757 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 500 |
| Chain | Residue |
| E | CYS42 |
| E | HIS65 |
| E | CYS152 |
| E | FU2600 |
| E | NAD1250 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 501 |
| Chain | Residue |
| E | CYS96 |
| E | GLY97 |
| E | CYS99 |
| E | CYS102 |
| E | CYS110 |
| site_id | CC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD E 1250 |
| Chain | Residue |
| C | VAL279 |
| E | HIS43 |
| E | THR44 |
| E | HIS47 |
| E | CYS152 |
| E | THR156 |
| E | GLY176 |
| E | ILE177 |
| E | GLY178 |
| E | GLY179 |
| E | LEU180 |
| E | ASP199 |
| E | ILE200 |
| E | LYS204 |
| E | THR241 |
| E | VAL243 |
| E | SER244 |
| E | ASN264 |
| E | GLY265 |
| E | LEU266 |
| E | SER288 |
| E | ILE289 |
| E | VAL290 |
| E | LEU327 |
| E | ARG335 |
| E | HOH352 |
| E | HOH353 |
| E | HOH362 |
| E | ZN500 |
| E | FU2600 |
| E | HOH694 |
| E | HOH806 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FU2 E 600 |
| Chain | Residue |
| E | THR44 |
| E | TRP53 |
| E | HIS65 |
| E | TRP91 |
| E | CYS152 |
| E | LEU266 |
| E | ILE289 |
| E | ZN500 |
| E | NAD1250 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 E 702 |
| Chain | Residue |
| E | PHE144 |
| E | VAL145 |
| E | HOH452 |
| E | HOH575 |
| G | ARG342 |
| G | SO4702 |
| G | HOH1332 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 500 |
| Chain | Residue |
| F | CYS42 |
| F | HIS65 |
| F | CYS152 |
| F | FU2600 |
| F | NAD1250 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 501 |
| Chain | Residue |
| F | CYS96 |
| F | GLY97 |
| F | CYS99 |
| F | CYS102 |
| F | CYS110 |
| site_id | DC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD F 1250 |
| Chain | Residue |
| F | HIS43 |
| F | THR44 |
| F | HIS47 |
| F | CYS152 |
| F | THR156 |
| F | GLY176 |
| F | ILE177 |
| F | GLY178 |
| F | GLY179 |
| F | LEU180 |
| F | ASP199 |
| F | ILE200 |
| F | LYS204 |
| F | THR241 |
| F | VAL243 |
| F | SER244 |
| F | ASN264 |
| F | GLY265 |
| F | LEU266 |
| F | SER288 |
| F | ILE289 |
| F | VAL290 |
| F | LEU327 |
| F | ARG335 |
| F | HOH354 |
| F | ZN500 |
| F | FU2600 |
| F | HOH1176 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FU2 F 600 |
| Chain | Residue |
| F | THR44 |
| F | TRP53 |
| F | HIS65 |
| F | TRP91 |
| F | CYS152 |
| F | LEU266 |
| F | ILE289 |
| F | ZN500 |
| F | NAD1250 |
| site_id | DC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 F 702 |
| Chain | Residue |
| F | GLY143 |
| F | PHE144 |
| F | VAL145 |
| F | HOH505 |
| F | HOH629 |
| H | ARG342 |
| H | SO4702 |
| H | HOH937 |
| H | HOH1289 |
| site_id | DC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD G 1250 |
| Chain | Residue |
| A | VAL279 |
| G | HIS43 |
| G | THR44 |
| G | HIS47 |
| G | THR156 |
| G | GLY176 |
| G | ILE177 |
| G | GLY178 |
| G | GLY179 |
| G | LEU180 |
| G | ASP199 |
| G | ILE200 |
| G | LYS204 |
| G | THR241 |
| G | ALA242 |
| G | VAL243 |
| G | SER244 |
| G | ALA247 |
| G | ASN264 |
| G | GLY265 |
| G | LEU266 |
| G | SER288 |
| G | ILE289 |
| G | VAL290 |
| G | LEU327 |
| G | ARG335 |
| G | HOH344 |
| G | HOH380 |
| G | HOH389 |
| G | HOH396 |
| G | ZN500 |
| G | FU2600 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 500 |
| Chain | Residue |
| G | CYS42 |
| G | HIS65 |
| G | CYS152 |
| G | FU2600 |
| G | NAD1250 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 501 |
| Chain | Residue |
| G | CYS96 |
| G | GLY97 |
| G | CYS99 |
| G | CYS102 |
| G | CYS110 |
| site_id | DC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FU2 G 600 |
| Chain | Residue |
| G | CYS42 |
| G | THR44 |
| G | TRP53 |
| G | HIS65 |
| G | TRP91 |
| G | CYS152 |
| G | LEU266 |
| G | ILE289 |
| G | VAL290 |
| G | ZN500 |
| G | NAD1250 |
| site_id | DC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 G 702 |
| Chain | Residue |
| E | GLY143 |
| E | HOH452 |
| E | SO4702 |
| G | ARG86 |
| G | GLY143 |
| G | PHE144 |
| G | HOH583 |
| G | HOH1129 |
| site_id | DC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 G 703 |
| Chain | Residue |
| G | ASN206 |
| G | ARG210 |
| G | HOH510 |
| G | HOH1259 |
| H | ARG209 |
| H | VAL215 |
| H | ALA216 |
| H | HOH600 |
| H | HOH902 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN H 500 |
| Chain | Residue |
| H | CYS42 |
| H | HIS65 |
| H | CYS152 |
| H | HOH1102 |
| H | NAD1250 |
| site_id | EC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN H 501 |
| Chain | Residue |
| H | CYS96 |
| H | GLY97 |
| H | CYS99 |
| H | CYS102 |
| H | CYS110 |
| site_id | EC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD H 1250 |
| Chain | Residue |
| H | HIS43 |
| H | THR44 |
| H | HIS47 |
| H | CYS152 |
| H | THR156 |
| H | GLY176 |
| H | ILE177 |
| H | GLY178 |
| H | GLY179 |
| H | LEU180 |
| H | ASP199 |
| H | ILE200 |
| H | LYS204 |
| H | THR241 |
| H | ALA242 |
| H | VAL243 |
| H | SER244 |
| H | ALA247 |
| H | ASN264 |
| H | GLY265 |
| H | LEU266 |
| H | SER288 |
| H | ILE289 |
| H | VAL290 |
| H | LEU327 |
| H | ARG335 |
| H | HOH352 |
| H | HOH364 |
| H | HOH377 |
| H | HOH394 |
| H | ZN500 |
| H | HOH546 |
| H | HOH1102 |
| H | HOH1104 |
| site_id | EC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 H 702 |
| Chain | Residue |
| F | GLU146 |
| F | HOH505 |
| F | SO4702 |
| H | ARG86 |
| H | GLY143 |
| H | PHE144 |
| H | HOH504 |
| H | HOH937 |
| site_id | EC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 H 703 |
| Chain | Residue |
| G | ARG209 |
| G | VAL215 |
| G | ALA216 |
| G | HOH399 |
| G | HOH881 |
| G | HOH1336 |
| H | ASN206 |
| H | ARG210 |
| H | HOH410 |
| H | HOH1013 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGYvsavGsgV |
| Chain | Residue | Details |
| A | GLY64-VAL78 |
