3S2I
Crystal Structure of FurX NADH+:Furfuryl alcohol II
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | HIS43 |
A | GLY179 |
A | ARG335 |
A | HOH380 |
A | HOH516 |
A | HOH676 |
A | HOH1329 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 702 |
Chain | Residue |
A | ARG86 |
A | GLY143 |
A | PHE144 |
A | HOH1457 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 500 |
Chain | Residue |
B | CYS42 |
B | HIS65 |
B | GLU66 |
B | CYS152 |
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 | 5 |
Details | BINDING SITE FOR RESIDUE FU2 B 600 |
Chain | Residue |
B | THR44 |
B | HIS65 |
B | TRP91 |
B | ILE289 |
H | LEU280 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 701 |
Chain | Residue |
B | CYS42 |
B | HIS43 |
B | GLY179 |
B | LEU180 |
B | ARG335 |
B | HOH371 |
B | HOH385 |
B | HOH506 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 702 |
Chain | Residue |
B | ARG86 |
B | PHE144 |
B | HOH823 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 500 |
Chain | Residue |
C | CYS42 |
C | HIS65 |
C | GLU66 |
C | CYS152 |
C | HOH788 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 501 |
Chain | Residue |
C | CYS96 |
C | CYS99 |
C | CYS102 |
C | CYS110 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FU2 C 600 |
Chain | Residue |
C | THR44 |
C | TRP91 |
C | LEU266 |
C | VAL290 |
C | HOH788 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 701 |
Chain | Residue |
C | HIS43 |
C | GLY179 |
C | ARG335 |
C | HOH759 |
C | HOH798 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 702 |
Chain | Residue |
C | ARG86 |
C | GLY143 |
C | PHE144 |
C | HOH957 |
C | HOH1214 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 500 |
Chain | Residue |
D | CYS42 |
D | HIS65 |
D | GLU66 |
D | CYS152 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 501 |
Chain | Residue |
D | CYS96 |
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 | ILE289 |
D | VAL290 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 701 |
Chain | Residue |
D | HIS43 |
D | GLY179 |
D | ARG335 |
D | HOH797 |
D | HOH847 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 702 |
Chain | Residue |
D | PHE144 |
D | HOH372 |
D | HOH446 |
D | ARG86 |
D | GLY143 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 500 |
Chain | Residue |
E | CYS42 |
E | HIS65 |
E | CYS152 |
E | FU2600 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 501 |
Chain | Residue |
E | CYS96 |
E | CYS99 |
E | CYS102 |
E | CYS110 |
site_id | CC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FU2 E 600 |
Chain | Residue |
E | CYS42 |
E | THR44 |
E | TRP53 |
E | HIS65 |
E | TRP91 |
E | CYS152 |
E | LEU266 |
E | ILE289 |
E | VAL290 |
E | ZN500 |
site_id | CC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 702 |
Chain | Residue |
E | GLY143 |
E | PHE144 |
E | VAL145 |
E | HOH378 |
E | HOH771 |
G | ARG342 |
G | SO4702 |
G | HOH875 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 500 |
Chain | Residue |
F | CYS42 |
F | HIS65 |
F | CYS152 |
F | FU2600 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 501 |
Chain | Residue |
F | CYS96 |
F | CYS99 |
F | CYS102 |
F | CYS110 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FU2 F 600 |
Chain | Residue |
F | THR44 |
F | HIS65 |
F | TRP91 |
F | CYS152 |
F | ILE289 |
F | VAL290 |
F | ZN500 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 F 702 |
Chain | Residue |
F | GLY143 |
F | PHE144 |
F | VAL145 |
F | HOH420 |
F | HOH923 |
H | ARG342 |
H | SO4702 |
H | HOH925 |
site_id | DC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD G 1250 |
Chain | Residue |
G | HIS43 |
G | THR44 |
G | HIS47 |
G | THR156 |
G | GLY176 |
G | GLY178 |
G | GLY179 |
G | LEU180 |
G | ASP199 |
G | ILE200 |
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 | HOH374 |
G | HOH379 |
G | HOH385 |
G | ZN500 |
G | HOH720 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN G 500 |
Chain | Residue |
G | CYS42 |
G | HIS65 |
G | CYS152 |
G | NAD1250 |
site_id | DC4 |
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 | DC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 702 |
Chain | Residue |
E | SO4702 |
G | GLY143 |
G | PHE144 |
site_id | DC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 G 703 |
Chain | Residue |
G | ASN206 |
G | ARG210 |
G | HOH810 |
G | HOH1277 |
H | ARG209 |
H | VAL215 |
H | ALA216 |
H | HOH859 |
site_id | DC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 500 |
Chain | Residue |
H | CYS42 |
H | HIS65 |
H | CYS152 |
H | NAD1250 |
site_id | DC8 |
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 | DC9 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD H 1250 |
Chain | Residue |
H | CYS42 |
H | HIS43 |
H | THR44 |
H | HIS47 |
H | CYS152 |
H | THR156 |
H | GLY176 |
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 | HOH363 |
H | HOH372 |
H | HOH444 |
H | ZN500 |
H | HOH826 |
H | HOH1137 |
site_id | EC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 702 |
Chain | Residue |
F | SO4702 |
H | ARG86 |
H | GLY143 |
H | PHE144 |
site_id | EC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 H 703 |
Chain | Residue |
G | ARG209 |
G | VAL215 |
G | ALA216 |
G | HOH391 |
H | ASN206 |
H | ARG210 |
H | HOH350 |
H | HOH935 |
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 |