4JBI
2.35A resolution structure of NADPH bound thermostable alcohol dehydrogenase from Pyrobaculum aerophilum
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 | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0043168 | molecular_function | anion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051262 | biological_process | protein tetramerization |
| 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| B | 0043168 | molecular_function | anion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051262 | biological_process | protein tetramerization |
| 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0043168 | molecular_function | anion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051262 | biological_process | protein tetramerization |
| 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| D | 0043168 | molecular_function | anion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051262 | biological_process | protein tetramerization |
| E | 0000166 | molecular_function | nucleotide 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| E | 0043168 | molecular_function | anion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051262 | biological_process | protein tetramerization |
| F | 0000166 | molecular_function | nucleotide 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| F | 0043168 | molecular_function | anion binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051262 | biological_process | protein tetramerization |
| G | 0000166 | molecular_function | nucleotide 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| G | 0043168 | molecular_function | anion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051262 | biological_process | protein tetramerization |
| H | 0000166 | molecular_function | nucleotide 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| H | 0043168 | molecular_function | anion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051262 | biological_process | protein tetramerization |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| I | 0030554 | molecular_function | adenyl nucleotide binding |
| I | 0043168 | molecular_function | anion binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051262 | biological_process | protein tetramerization |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| J | 0030554 | molecular_function | adenyl nucleotide binding |
| J | 0043168 | molecular_function | anion binding |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0051262 | biological_process | protein tetramerization |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| K | 0030554 | molecular_function | adenyl nucleotide binding |
| K | 0043168 | molecular_function | anion binding |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0051262 | biological_process | protein tetramerization |
| L | 0000166 | molecular_function | nucleotide binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| L | 0030554 | molecular_function | adenyl nucleotide binding |
| L | 0043168 | molecular_function | anion binding |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051262 | biological_process | protein tetramerization |
| M | 0000166 | molecular_function | nucleotide binding |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| M | 0030554 | molecular_function | adenyl nucleotide binding |
| M | 0043168 | molecular_function | anion binding |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0051262 | biological_process | protein tetramerization |
| N | 0000166 | molecular_function | nucleotide binding |
| N | 0016491 | molecular_function | oxidoreductase activity |
| N | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| N | 0030554 | molecular_function | adenyl nucleotide binding |
| N | 0043168 | molecular_function | anion binding |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0051262 | biological_process | protein tetramerization |
| O | 0000166 | molecular_function | nucleotide binding |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| O | 0030554 | molecular_function | adenyl nucleotide binding |
| O | 0043168 | molecular_function | anion binding |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0051262 | biological_process | protein tetramerization |
| P | 0000166 | molecular_function | nucleotide binding |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| P | 0030554 | molecular_function | adenyl nucleotide binding |
| P | 0043168 | molecular_function | anion binding |
| P | 0046872 | molecular_function | metal ion binding |
| P | 0051262 | biological_process | protein tetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP A 401 |
| Chain | Residue |
| A | PRO40 |
| A | SER195 |
| A | ARG196 |
| A | ARG197 |
| A | PRO231 |
| A | THR232 |
| A | SER236 |
| A | ALA253 |
| A | GLY254 |
| A | ALA255 |
| A | LEU256 |
| A | ARG88 |
| A | THR257 |
| A | THR279 |
| A | GLY280 |
| A | ARG323 |
| A | HOH509 |
| A | HOH516 |
| A | HOH523 |
| A | HOH536 |
| A | HOH539 |
| A | ILE147 |
| A | THR151 |
| A | GLY171 |
| A | THR173 |
| A | GLY174 |
| A | ASN175 |
| A | VAL176 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | CYS91 |
| A | CYS94 |
| A | CYS97 |
| A | CYS105 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP B 401 |
| Chain | Residue |
| B | PRO40 |
| B | ARG88 |
| B | ILE147 |
| B | THR151 |
| B | GLY171 |
| B | THR173 |
| B | GLY174 |
| B | ASN175 |
| B | VAL176 |
| B | SER195 |
| B | ARG196 |
| B | ARG197 |
| B | PRO231 |
| B | THR232 |
| B | ALA253 |
| B | GLY254 |
| B | ALA255 |
| B | LEU256 |
| B | THR257 |
| B | THR279 |
| B | GLY280 |
| B | ARG323 |
| B | HOH505 |
| B | HOH527 |
| B | HOH534 |
| B | HOH554 |
| B | HOH560 |
| B | HOH587 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | CYS91 |
| B | CYS94 |
| B | CYS97 |
| B | CYS105 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NDP C 401 |
| Chain | Residue |
| C | PRO40 |
| C | ILE147 |
| C | THR151 |
| C | GLY171 |
| C | THR173 |
| C | GLY174 |
| C | ASN175 |
| C | VAL176 |
| C | SER195 |
| C | ARG196 |
| C | ARG197 |
| C | PRO231 |
| C | THR232 |
| C | ALA253 |
| C | GLY254 |
| C | ALA255 |
| C | LEU256 |
| C | THR257 |
| C | THR279 |
| C | GLY280 |
| C | ARG323 |
| C | HOH506 |
| C | HOH517 |
| C | HOH528 |
| C | HOH536 |
| C | HOH567 |
| C | HOH585 |
| C | HOH587 |
| H | ARG79 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 402 |
| Chain | Residue |
| C | CYS91 |
| C | CYS94 |
| C | CYS97 |
| C | CYS105 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP D 401 |
| Chain | Residue |
| D | ILE147 |
| D | THR151 |
| D | GLY171 |
| D | THR173 |
| D | GLY174 |
| D | ASN175 |
| D | VAL176 |
| D | SER195 |
| D | ARG196 |
| D | ARG197 |
| D | PRO231 |
| D | THR232 |
| D | ALA253 |
| D | GLY254 |
| D | LEU256 |
| D | THR257 |
| D | THR279 |
| D | GLY280 |
| D | ARG323 |
| D | HOH506 |
| D | HOH510 |
| D | HOH511 |
| D | HOH514 |
| D | HOH535 |
| D | HOH536 |
| D | HOH539 |
| D | HOH560 |
| D | HOH570 |
| D | PRO40 |
| D | ARG88 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 402 |
| Chain | Residue |
| D | CYS91 |
| D | CYS94 |
| D | CYS97 |
| D | CYS105 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP E 401 |
| Chain | Residue |
| E | PRO40 |
| E | ARG88 |
| E | ILE147 |
| E | THR151 |
| E | GLY171 |
| E | THR173 |
| E | GLY174 |
| E | ASN175 |
| E | VAL176 |
| E | SER195 |
| E | ARG196 |
| E | ARG197 |
| E | PRO231 |
| E | THR232 |
| E | ALA253 |
| E | GLY254 |
| E | ALA255 |
| E | LEU256 |
| E | THR257 |
| E | THR279 |
| E | GLY280 |
| E | ARG323 |
| E | HOH506 |
| E | HOH513 |
| E | HOH542 |
| E | HOH573 |
| E | HOH578 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 402 |
| Chain | Residue |
| E | CYS91 |
| E | CYS94 |
| E | CYS97 |
| E | CYS105 |
| site_id | BC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NDP F 401 |
| Chain | Residue |
| F | PRO40 |
| F | ILE147 |
| F | THR151 |
| F | GLY171 |
| F | THR173 |
| F | GLY174 |
| F | ASN175 |
| F | VAL176 |
| F | SER195 |
| F | ARG196 |
| F | ARG197 |
| F | PRO231 |
| F | THR232 |
| F | SER236 |
| F | ALA253 |
| F | GLY254 |
| F | ALA255 |
| F | LEU256 |
| F | THR257 |
| F | THR279 |
| F | GLY280 |
| F | ARG323 |
| F | HOH501 |
| F | HOH510 |
| F | HOH526 |
| F | HOH563 |
| F | HOH578 |
| F | HOH579 |
| I | ARG79 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 402 |
| Chain | Residue |
| F | CYS91 |
| F | CYS94 |
| F | CYS97 |
| F | CYS105 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP G 401 |
| Chain | Residue |
| G | PRO40 |
| G | ARG88 |
| G | ILE147 |
| G | THR151 |
| G | GLY171 |
| G | THR173 |
| G | GLY174 |
| G | ASN175 |
| G | VAL176 |
| G | SER195 |
| G | ARG196 |
| G | ARG197 |
| G | PRO231 |
| G | THR232 |
| G | ALA253 |
| G | GLY254 |
| G | ALA255 |
| G | LEU256 |
| G | THR257 |
| G | THR279 |
| G | GLY280 |
| G | ARG323 |
| G | HOH503 |
| G | HOH516 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN G 402 |
| Chain | Residue |
| G | CYS91 |
| G | CYS94 |
| G | CYS97 |
| G | CYS105 |
| site_id | BC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NDP H 401 |
| Chain | Residue |
| H | PRO40 |
| H | ARG88 |
| H | ILE147 |
| H | THR151 |
| H | GLY171 |
| H | THR173 |
| H | GLY174 |
| H | ASN175 |
| H | VAL176 |
| H | SER195 |
| H | ARG196 |
| H | ARG197 |
| H | PRO231 |
| H | THR232 |
| H | SER236 |
| H | ALA253 |
| H | GLY254 |
| H | ALA255 |
| H | LEU256 |
| H | THR257 |
| H | THR279 |
| H | GLY280 |
| H | ARG323 |
| H | HOH502 |
| H | HOH511 |
| H | HOH532 |
| H | HOH548 |
| H | HOH550 |
| H | HOH565 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 402 |
| Chain | Residue |
| H | CYS91 |
| H | CYS94 |
| H | CYS97 |
| H | CYS105 |
| site_id | BC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP I 401 |
| Chain | Residue |
| I | PRO40 |
| I | ARG88 |
| I | ILE147 |
| I | THR151 |
| I | GLY171 |
| I | THR173 |
| I | GLY174 |
| I | ASN175 |
| I | VAL176 |
| I | SER195 |
| I | ARG196 |
| I | ARG197 |
| I | PRO231 |
| I | THR232 |
| I | SER236 |
| I | ALA253 |
| I | GLY254 |
| I | ALA255 |
| I | LEU256 |
| I | THR257 |
| I | THR279 |
| I | GLY280 |
| I | ARG323 |
| I | HOH502 |
| I | HOH525 |
| I | HOH528 |
| I | HOH563 |
| O | TYR269 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 402 |
| Chain | Residue |
| I | CYS91 |
| I | CYS94 |
| I | CYS97 |
| I | CYS105 |
| site_id | CC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP J 401 |
| Chain | Residue |
| J | PRO40 |
| J | ARG88 |
| J | ILE147 |
| J | THR151 |
| J | GLY171 |
| J | THR173 |
| J | GLY174 |
| J | ASN175 |
| J | VAL176 |
| J | SER195 |
| J | ARG196 |
| J | ARG197 |
| J | PRO231 |
| J | THR232 |
| J | ALA253 |
| J | GLY254 |
| J | ALA255 |
| J | LEU256 |
| J | THR257 |
| J | THR279 |
| J | GLY280 |
| J | ARG323 |
| J | HOH520 |
| J | HOH521 |
| J | HOH532 |
| J | HOH563 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN J 402 |
| Chain | Residue |
| J | CYS91 |
| J | CYS94 |
| J | CYS97 |
| J | CYS105 |
| site_id | CC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP K 401 |
| Chain | Residue |
| K | PRO40 |
| K | ARG88 |
| K | ILE147 |
| K | THR151 |
| K | GLY171 |
| K | THR173 |
| K | GLY174 |
| K | ASN175 |
| K | VAL176 |
| K | SER195 |
| K | ARG196 |
| K | ARG197 |
| K | PRO231 |
| K | THR232 |
| K | ALA253 |
| K | GLY254 |
| K | ALA255 |
| K | LEU256 |
| K | THR257 |
| K | THR279 |
| K | GLY280 |
| K | ARG323 |
| K | HOH502 |
| K | HOH539 |
| K | HOH543 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN K 402 |
| Chain | Residue |
| K | CYS91 |
| K | CYS94 |
| K | CYS97 |
| K | CYS105 |
| site_id | CC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP L 401 |
| Chain | Residue |
| L | PRO40 |
| L | ILE147 |
| L | THR151 |
| L | GLY171 |
| L | THR173 |
| L | GLY174 |
| L | ASN175 |
| L | VAL176 |
| L | SER195 |
| L | ARG196 |
| L | ARG197 |
| L | PRO231 |
| L | THR232 |
| L | ALA253 |
| L | GLY254 |
| L | ALA255 |
| L | LEU256 |
| L | THR257 |
| L | THR279 |
| L | GLY280 |
| L | ARG323 |
| L | HOH501 |
| L | HOH517 |
| L | HOH521 |
| L | HOH525 |
| L | HOH541 |
| L | HOH548 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN L 402 |
| Chain | Residue |
| L | CYS91 |
| L | CYS94 |
| L | CYS97 |
| L | CYS105 |
| site_id | CC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP M 401 |
| Chain | Residue |
| M | PRO40 |
| M | ILE147 |
| M | THR151 |
| M | GLY171 |
| M | THR173 |
| M | GLY174 |
| M | ASN175 |
| M | VAL176 |
| M | SER195 |
| M | ARG196 |
| M | ARG197 |
| M | PRO231 |
| M | SER236 |
| M | ALA253 |
| M | GLY254 |
| M | ALA255 |
| M | LEU256 |
| M | THR257 |
| M | THR279 |
| M | GLY280 |
| M | ARG323 |
| M | HOH501 |
| M | HOH518 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN M 402 |
| Chain | Residue |
| M | CYS91 |
| M | GLY92 |
| M | CYS94 |
| M | CYS97 |
| M | CYS105 |
| site_id | CC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP N 401 |
| Chain | Residue |
| N | PRO40 |
| N | ILE147 |
| N | THR151 |
| N | GLY171 |
| N | THR173 |
| N | GLY174 |
| N | ASN175 |
| N | VAL176 |
| N | SER195 |
| N | ARG196 |
| N | ARG197 |
| N | PRO231 |
| N | THR232 |
| N | SER236 |
| N | ALA253 |
| N | GLY254 |
| N | ALA255 |
| N | LEU256 |
| N | THR257 |
| N | THR279 |
| N | GLY280 |
| N | ARG323 |
| N | HOH502 |
| N | HOH513 |
| N | HOH516 |
| N | HOH525 |
| N | HOH551 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN N 402 |
| Chain | Residue |
| N | CYS91 |
| N | CYS94 |
| N | CYS97 |
| N | CYS105 |
| site_id | DC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP O 401 |
| Chain | Residue |
| O | PRO40 |
| O | ARG88 |
| O | ILE147 |
| O | THR151 |
| O | GLY171 |
| O | THR173 |
| O | GLY174 |
| O | ASN175 |
| O | VAL176 |
| O | SER195 |
| O | ARG196 |
| O | ARG197 |
| O | PRO231 |
| O | THR232 |
| O | ALA253 |
| O | GLY254 |
| O | ALA255 |
| O | LEU256 |
| O | THR257 |
| O | THR279 |
| O | GLY280 |
| O | ARG323 |
| O | HOH534 |
| O | HOH544 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN O 402 |
| Chain | Residue |
| O | CYS91 |
| O | CYS94 |
| O | CYS97 |
| O | CYS105 |
| site_id | DC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP P 401 |
| Chain | Residue |
| P | PRO40 |
| P | ILE147 |
| P | THR151 |
| P | GLY171 |
| P | THR173 |
| P | GLY174 |
| P | ASN175 |
| P | VAL176 |
| P | SER195 |
| P | ARG196 |
| P | ARG197 |
| P | PRO231 |
| P | THR232 |
| P | SER236 |
| P | ALA253 |
| P | GLY254 |
| P | ALA255 |
| P | LEU256 |
| P | THR257 |
| P | THR279 |
| P | GLY280 |
| P | ARG323 |
| P | HOH501 |
| P | HOH513 |
| P | HOH526 |
| P | HOH540 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN P 402 |
| Chain | Residue |
| P | CYS91 |
| P | CYS94 |
| P | CYS97 |
| P | CYS105 |
