4GH5
Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0048038 | molecular_function | quinone binding |
| A | 0050575 | molecular_function | 2-(S)-hydroxypropyl-CoM dehydrogenase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0048038 | molecular_function | quinone binding |
| B | 0050575 | molecular_function | 2-(S)-hydroxypropyl-CoM dehydrogenase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0048038 | molecular_function | quinone binding |
| C | 0050575 | molecular_function | 2-(S)-hydroxypropyl-CoM dehydrogenase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0048038 | molecular_function | quinone binding |
| D | 0050575 | molecular_function | 2-(S)-hydroxypropyl-CoM dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | GLY14 |
| A | ASN91 |
| A | GLY93 |
| A | ARG110 |
| A | VAL114 |
| A | PHE141 |
| A | GLY142 |
| A | SER143 |
| A | TYR156 |
| A | LYS160 |
| A | PRO186 |
| A | GLY18 |
| A | GLY187 |
| A | THR188 |
| A | VAL189 |
| A | THR192 |
| A | GLY193 |
| A | MET194 |
| A | ACT302 |
| A | HOH406 |
| A | HOH428 |
| A | HOH435 |
| A | ILE19 |
| A | HOH438 |
| A | HOH446 |
| A | HOH467 |
| A | HOH491 |
| A | HOH519 |
| A | ASP38 |
| A | LEU39 |
| A | LEU43 |
| A | ALA63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | SER143 |
| A | TYR156 |
| A | LEU198 |
| A | NAD301 |
| A | HOH465 |
| A | HOH612 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 301 |
| Chain | Residue |
| B | GLY14 |
| B | GLY18 |
| B | ILE19 |
| B | ASP38 |
| B | LEU39 |
| B | ALA63 |
| B | ASP64 |
| B | VAL65 |
| B | ASN91 |
| B | GLY93 |
| B | ARG110 |
| B | VAL114 |
| B | PHE141 |
| B | GLY142 |
| B | SER143 |
| B | TYR156 |
| B | LYS160 |
| B | PRO186 |
| B | GLY187 |
| B | THR188 |
| B | VAL189 |
| B | THR192 |
| B | GLY193 |
| B | MET194 |
| B | ACT302 |
| B | HOH418 |
| B | HOH445 |
| B | HOH448 |
| B | HOH457 |
| B | HOH460 |
| B | HOH471 |
| B | HOH474 |
| B | HOH503 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | SER143 |
| B | TYR156 |
| B | LEU198 |
| B | NAD301 |
| B | HOH489 |
| B | HOH580 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD C 301 |
| Chain | Residue |
| C | VAL189 |
| C | THR192 |
| C | GLY193 |
| C | MET194 |
| C | ACT302 |
| C | HOH411 |
| C | HOH437 |
| C | HOH438 |
| C | HOH470 |
| C | HOH471 |
| C | HOH476 |
| C | HOH502 |
| C | HOH505 |
| C | GLY14 |
| C | GLY18 |
| C | ILE19 |
| C | ASP38 |
| C | LEU39 |
| C | ALA63 |
| C | ASP64 |
| C | VAL65 |
| C | ASN91 |
| C | GLY93 |
| C | ARG110 |
| C | VAL114 |
| C | PHE141 |
| C | GLY142 |
| C | SER143 |
| C | TYR156 |
| C | LYS160 |
| C | PRO186 |
| C | GLY187 |
| C | THR188 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 302 |
| Chain | Residue |
| C | SER143 |
| C | TYR156 |
| C | LEU198 |
| C | NAD301 |
| C | HOH495 |
| C | HOH585 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD D 301 |
| Chain | Residue |
| D | GLY14 |
| D | GLY18 |
| D | ILE19 |
| D | ASP38 |
| D | LEU39 |
| D | ALA63 |
| D | ASP64 |
| D | VAL65 |
| D | ASN91 |
| D | GLY93 |
| D | ARG110 |
| D | VAL114 |
| D | PHE141 |
| D | GLY142 |
| D | SER143 |
| D | TYR156 |
| D | LYS160 |
| D | PRO186 |
| D | GLY187 |
| D | THR188 |
| D | VAL189 |
| D | THR192 |
| D | GLY193 |
| D | MET194 |
| D | ACT302 |
| D | HOH405 |
| D | HOH428 |
| D | HOH439 |
| D | HOH448 |
| D | HOH470 |
| D | HOH473 |
| D | HOH480 |
| D | HOH486 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 302 |
| Chain | Residue |
| D | SER143 |
| D | TYR156 |
| D | LEU198 |
| D | NAD301 |
| D | HOH579 |
| D | HOH585 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvaglvgiptMaaYCAAKGAIvNLTrQMA |
| Chain | Residue | Details |
| A | SER143-ALA171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20302306","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23474457","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23474457","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GH5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ITU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23474457","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ITU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"20302306","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23474457","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"20302306","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23474457","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
