5HWS
Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0015940 | biological_process | pantothenate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0015940 | biological_process | pantothenate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0015940 | biological_process | pantothenate biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0015940 | biological_process | pantothenate biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | GLY7 |
| A | LYS74 |
| A | SER77 |
| A | ALA81 |
| A | GLN99 |
| A | ASN100 |
| A | THR120 |
| A | ASN122 |
| A | GLY123 |
| A | ALA124 |
| A | GLU262 |
| A | GLY9 |
| A | HOH508 |
| A | HOH523 |
| A | HOH525 |
| A | HOH535 |
| A | HOH538 |
| A | HOH553 |
| A | HOH558 |
| A | HOH567 |
| A | SER10 |
| A | ILE11 |
| A | ILE29 |
| A | GLY30 |
| A | ARG31 |
| A | ALA72 |
| A | VAL73 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| B | GLY7 |
| B | GLY9 |
| B | SER10 |
| B | ILE11 |
| B | GLY30 |
| B | ARG31 |
| B | ALA72 |
| B | VAL73 |
| B | LYS74 |
| B | ALA81 |
| B | ASN100 |
| B | THR120 |
| B | ASN122 |
| B | GLY123 |
| B | ALA124 |
| B | GLU262 |
| B | HOH505 |
| B | HOH549 |
| B | HOH558 |
| B | HOH575 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue NAP C 401 |
| Chain | Residue |
| C | GLY7 |
| C | GLY9 |
| C | SER10 |
| C | ILE11 |
| C | ILE29 |
| C | GLY30 |
| C | ARG31 |
| C | ALA72 |
| C | LYS74 |
| C | ALA81 |
| C | GLN99 |
| C | ASN100 |
| C | THR120 |
| C | ASN122 |
| C | ALA124 |
| C | GLU262 |
| C | HOH515 |
| C | HOH534 |
| C | HOH540 |
| C | HOH542 |
| C | HOH551 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue NAP D 401 |
| Chain | Residue |
| D | GLY7 |
| D | GLY9 |
| D | SER10 |
| D | ILE11 |
| D | ILE29 |
| D | GLY30 |
| D | ARG31 |
| D | ALA72 |
| D | VAL73 |
| D | LYS74 |
| D | ALA81 |
| D | ILE98 |
| D | GLN99 |
| D | ASN100 |
| D | THR120 |
| D | ASN122 |
| D | ALA124 |
| D | GLU262 |
| D | HOH508 |
| D | HOH512 |
| D | HOH539 |
| D | HOH541 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A9J4 |
| Chain | Residue | Details |
| A | LYS180 | |
| B | LYS180 | |
| C | LYS180 | |
| D | LYS180 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26757028, ECO:0000269|PubMed:27139828 |
| Chain | Residue | Details |
| A | GLY7 | |
| C | ASN100 | |
| C | ALA124 | |
| C | GLU262 | |
| D | GLY7 | |
| D | ASN100 | |
| D | ALA124 | |
| D | GLU262 | |
| A | ASN100 | |
| A | ALA124 | |
| A | GLU262 | |
| B | GLY7 | |
| B | ASN100 | |
| B | ALA124 | |
| B | GLU262 | |
| C | GLY7 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26757028 |
| Chain | Residue | Details |
| A | ALA8 | |
| B | ALA8 | |
| B | ARG31 | |
| B | ALA84 | |
| B | LYS180 | |
| B | ASN184 | |
| B | ASN188 | |
| B | ASN198 | |
| B | ASN247 | |
| B | ARG257 | |
| C | ALA8 | |
| A | ARG31 | |
| C | ARG31 | |
| C | ALA84 | |
| C | LYS180 | |
| C | ASN184 | |
| C | ASN188 | |
| C | ASN198 | |
| C | ASN247 | |
| C | ARG257 | |
| D | ALA8 | |
| D | ARG31 | |
| A | ALA84 | |
| D | ALA84 | |
| D | LYS180 | |
| D | ASN184 | |
| D | ASN188 | |
| D | ASN198 | |
| D | ASN247 | |
| D | ARG257 | |
| A | LYS180 | |
| A | ASN184 | |
| A | ASN188 | |
| A | ASN198 | |
| A | ASN247 | |
| A | ARG257 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27139828 |
| Chain | Residue | Details |
| A | LYS74 | |
| B | LYS74 | |
| C | LYS74 | |
| D | LYS74 |
