1YE4
Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| A | 0042732 | biological_process | D-xylose metabolic process |
| A | 0042843 | biological_process | D-xylose catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| B | 0042732 | biological_process | D-xylose metabolic process |
| B | 0042843 | biological_process | D-xylose catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| C | 0042732 | biological_process | D-xylose metabolic process |
| C | 0042843 | biological_process | D-xylose catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0032866 | molecular_function | D-xylose reductase (NADPH) activity |
| D | 0042732 | biological_process | D-xylose metabolic process |
| D | 0042843 | biological_process | D-xylose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | LYS25 |
| B | LEU26 |
| B | ALA27 |
| B | GLN34 |
| B | ARG274 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 D 902 |
| Chain | Residue |
| D | ARG232 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 903 |
| Chain | Residue |
| C | HIS14 |
| C | LEU15 |
| C | HOH1011 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 904 |
| Chain | Residue |
| A | HIS14 |
| A | LEU15 |
| A | HOH921 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 905 |
| Chain | Residue |
| B | HIS14 |
| B | LEU15 |
| B | HOH942 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 906 |
| Chain | Residue |
| D | LYS25 |
| D | LEU26 |
| D | ALA27 |
| D | THR30 |
| D | GLN34 |
| D | ARG274 |
| D | HOH969 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD A 800 |
| Chain | Residue |
| A | GLY22 |
| A | CYS23 |
| A | TRP24 |
| A | ASP47 |
| A | TYR52 |
| A | LYS81 |
| A | HIS114 |
| A | SER169 |
| A | ASN170 |
| A | GLN191 |
| A | TYR217 |
| A | SER218 |
| A | SER219 |
| A | PHE220 |
| A | GLN223 |
| A | SER224 |
| A | GLU227 |
| A | ALA257 |
| A | ILE272 |
| A | PRO273 |
| A | ARG274 |
| A | ASN276 |
| A | ARG280 |
| A | ASN284 |
| A | HOH910 |
| site_id | AC8 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 801 |
| Chain | Residue |
| B | GLY22 |
| B | CYS23 |
| B | TRP24 |
| B | ASP47 |
| B | TYR52 |
| B | LYS81 |
| B | HIS114 |
| B | SER169 |
| B | ASN170 |
| B | GLN191 |
| B | TYR217 |
| B | SER218 |
| B | SER219 |
| B | PHE220 |
| B | GLN223 |
| B | SER224 |
| B | GLU227 |
| B | ASN229 |
| B | PHE240 |
| B | ALA257 |
| B | ILE272 |
| B | PRO273 |
| B | ARG274 |
| B | ASN276 |
| B | ARG280 |
| B | ASN284 |
| B | ASN310 |
| B | HOH907 |
| B | HOH922 |
| B | HOH924 |
| B | HOH946 |
| B | HOH952 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 802 |
| Chain | Residue |
| C | PRO273 |
| C | ARG274 |
| C | ASN276 |
| C | ARG280 |
| C | ASN284 |
| C | ASN310 |
| C | HOH918 |
| C | GLY22 |
| C | CYS23 |
| C | TRP24 |
| C | ASP47 |
| C | TYR52 |
| C | LYS81 |
| C | HIS114 |
| C | SER169 |
| C | ASN170 |
| C | GLN191 |
| C | TYR217 |
| C | SER218 |
| C | SER219 |
| C | PHE220 |
| C | GLN223 |
| C | SER224 |
| C | GLU227 |
| C | PHE240 |
| C | ALA257 |
| C | ILE272 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 803 |
| Chain | Residue |
| D | GLY22 |
| D | CYS23 |
| D | TRP24 |
| D | ASP47 |
| D | TYR52 |
| D | LYS81 |
| D | HIS114 |
| D | SER169 |
| D | ASN170 |
| D | GLN191 |
| D | TYR217 |
| D | SER218 |
| D | SER219 |
| D | PHE220 |
| D | GLN223 |
| D | SER224 |
| D | GLU227 |
| D | ASN229 |
| D | PHE240 |
| D | ILE272 |
| D | PRO273 |
| D | ARG274 |
| D | ASN276 |
| D | ARG280 |
| D | GLN283 |
| D | ASN284 |
| D | ASN310 |
| D | HOH912 |
| D | HOH934 |
| D | HOH1020 |
| D | HOH1024 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeklvaagkIKSIGVSNF |
| Chain | Residue | Details |
| A | LEU154-PHE171 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPRSNLpeRLvQNrSF |
| Chain | Residue | Details |
| A | ILE272-PHE287 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRLFDGAedygnEkeVG |
| Chain | Residue | Details |
| A | GLY42-GLY59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | TYR52 | |
| B | TYR52 | |
| C | TYR52 | |
| D | TYR52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS114 | |
| B | HIS114 | |
| C | HIS114 | |
| D | HIS114 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12733986, ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198 |
| Chain | Residue | Details |
| A | SER169 | |
| D | SER169 | |
| D | SER218 | |
| D | ARG274 | |
| A | SER218 | |
| A | ARG274 | |
| B | SER169 | |
| B | SER218 | |
| B | ARG274 | |
| C | SER169 | |
| C | SER218 | |
| C | ARG274 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS81 | |
| B | LYS81 | |
| C | LYS81 | |
| D | LYS81 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS81 | |
| A | ASP47 | |
| A | HIS114 | |
| A | TYR52 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | LYS81 | |
| B | ASP47 | |
| B | HIS114 | |
| B | TYR52 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | LYS81 | |
| C | ASP47 | |
| C | HIS114 | |
| C | TYR52 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | LYS81 | |
| D | ASP47 | |
| D | HIS114 | |
| D | TYR52 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS81 | |
| A | TYR52 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | LYS81 | |
| B | TYR52 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | LYS81 | |
| C | TYR52 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | LYS81 | |
| D | TYR52 |
