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 |