4M55
Crystal structure of Human UDP-xylose synthase R236H substitution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0042732 | biological_process | D-xylose metabolic process |
| A | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0042732 | biological_process | D-xylose metabolic process |
| B | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0042732 | biological_process | D-xylose metabolic process |
| C | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| C | 0070403 | molecular_function | NAD+ binding |
| D | 0042732 | biological_process | D-xylose metabolic process |
| D | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| D | 0070403 | molecular_function | NAD+ binding |
| E | 0042732 | biological_process | D-xylose metabolic process |
| E | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| E | 0070403 | molecular_function | NAD+ binding |
| F | 0042732 | biological_process | D-xylose metabolic process |
| F | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| F | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | GLY95 |
| A | THR123 |
| A | GLY124 |
| A | HIS143 |
| A | ASP144 |
| A | VAL145 |
| A | LEU159 |
| A | ALA160 |
| A | SER161 |
| A | THR178 |
| A | ALA200 |
| A | ALA97 |
| A | SER201 |
| A | THR202 |
| A | LYS235 |
| A | ILE258 |
| A | PHE259 |
| A | THR261 |
| A | HIS267 |
| A | GLY98 |
| A | PHE99 |
| A | VAL100 |
| A | ASP119 |
| A | ASN120 |
| A | PHE121 |
| A | PHE122 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP A 502 |
| Chain | Residue |
| A | LYS191 |
| A | TYR245 |
| B | LYS177 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | HIS267 |
| A | MET268 |
| A | ASN269 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | GLY95 |
| B | ALA97 |
| B | GLY98 |
| B | PHE99 |
| B | VAL100 |
| B | ASP119 |
| B | ASN120 |
| B | PHE121 |
| B | PHE122 |
| B | THR123 |
| B | GLY124 |
| B | HIS143 |
| B | ASP144 |
| B | VAL145 |
| B | LEU159 |
| B | SER161 |
| B | PRO162 |
| B | THR178 |
| B | THR202 |
| B | LYS235 |
| B | ILE258 |
| B | THR261 |
| B | HIS267 |
| B | ARG272 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE UDP B 502 |
| Chain | Residue |
| A | LYS177 |
| B | PRO148 |
| B | LEU149 |
| B | TYR150 |
| B | LEU184 |
| B | ASN185 |
| B | GLY188 |
| B | LEU189 |
| B | LYS191 |
| B | ARG192 |
| B | TYR245 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | HIS267 |
| B | MET268 |
| B | ASN269 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | GLY95 |
| C | ALA97 |
| C | GLY98 |
| C | PHE99 |
| C | VAL100 |
| C | ASP119 |
| C | ASN120 |
| C | PHE121 |
| C | PHE122 |
| C | THR123 |
| C | GLY124 |
| C | HIS143 |
| C | ASP144 |
| C | VAL145 |
| C | LEU159 |
| C | ALA160 |
| C | SER161 |
| C | PRO162 |
| C | ALA163 |
| C | THR178 |
| C | ALA200 |
| C | THR202 |
| C | LYS235 |
| C | ILE258 |
| C | THR261 |
| C | HIS267 |
| C | ARG272 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE POP C 502 |
| Chain | Residue |
| C | TYR245 |
| D | LYS177 |
| C | GLY188 |
| C | LYS191 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 503 |
| Chain | Residue |
| C | HIS267 |
| C | MET268 |
| C | ASN269 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D 501 |
| Chain | Residue |
| D | GLY95 |
| D | ALA97 |
| D | GLY98 |
| D | PHE99 |
| D | VAL100 |
| D | GLY101 |
| D | ASP119 |
| D | ASN120 |
| D | PHE121 |
| D | PHE122 |
| D | THR123 |
| D | GLY124 |
| D | HIS143 |
| D | ASP144 |
| D | VAL145 |
| D | LEU159 |
| D | ALA160 |
| D | SER161 |
| D | THR178 |
| D | ALA200 |
| D | THR202 |
| D | LYS235 |
| D | ILE258 |
| D | PHE259 |
| D | THR261 |
| D | HIS267 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UDP D 502 |
| Chain | Residue |
| C | LYS177 |
| D | PRO148 |
| D | LEU184 |
| D | ASN185 |
| D | GLY188 |
| D | LYS191 |
| D | TYR245 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD E 800 |
| Chain | Residue |
| E | GLY95 |
| E | ALA97 |
| E | GLY98 |
| E | PHE99 |
| E | VAL100 |
| E | ASP119 |
| E | ASN120 |
| E | PHE121 |
| E | PHE122 |
| E | THR123 |
| E | GLY124 |
| E | HIS143 |
| E | ASP144 |
| E | VAL145 |
| E | LEU159 |
| E | SER161 |
| E | PRO162 |
| E | THR178 |
| E | THR202 |
| E | PHE259 |
| E | THR261 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD F 800 |
| Chain | Residue |
| F | ALA97 |
| F | GLY98 |
| F | PHE99 |
| F | VAL100 |
| F | ASP119 |
| F | ASN120 |
| F | PHE121 |
| F | PHE122 |
| F | THR123 |
| F | GLY124 |
| F | HIS143 |
| F | ASP144 |
| F | VAL145 |
| F | LYS174 |
| F | THR178 |
| F | THR261 |
| F | HIS267 |
| F | ARG272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:23656592, ECO:0000269|PubMed:25521717 |
| Chain | Residue | Details |
| A | TYR231 | |
| B | TYR231 | |
| C | TYR231 | |
| D | TYR231 | |
| E | TYR231 | |
| F | TYR231 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 90 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22810237, ECO:0000269|PubMed:25521717, ECO:0007744|PDB:2B69, ECO:0007744|PDB:4LK3, ECO:0007744|PDB:4M55 |
| Chain | Residue | Details |
| A | GLY98 | |
| A | VAL145 | |
| A | LEU159 | |
| A | THR178 | |
| A | LYS235 | |
| A | THR261 | |
| A | ARG272 | |
| B | GLY98 | |
| B | PHE99 | |
| B | VAL100 | |
| B | ASP119 | |
| A | PHE99 | |
| B | ASN120 | |
| B | PHE122 | |
| B | THR123 | |
| B | GLY124 | |
| B | ASP144 | |
| B | VAL145 | |
| B | LEU159 | |
| B | THR178 | |
| B | LYS235 | |
| B | THR261 | |
| A | VAL100 | |
| B | ARG272 | |
| C | GLY98 | |
| C | PHE99 | |
| C | VAL100 | |
| C | ASP119 | |
| C | ASN120 | |
| C | PHE122 | |
| C | THR123 | |
| C | GLY124 | |
| C | ASP144 | |
| A | ASP119 | |
| C | VAL145 | |
| C | LEU159 | |
| C | THR178 | |
| C | LYS235 | |
| C | THR261 | |
| C | ARG272 | |
| D | GLY98 | |
| D | PHE99 | |
| D | VAL100 | |
| D | ASP119 | |
| A | ASN120 | |
| D | ASN120 | |
| D | PHE122 | |
| D | THR123 | |
| D | GLY124 | |
| D | ASP144 | |
| D | VAL145 | |
| D | LEU159 | |
| D | THR178 | |
| D | LYS235 | |
| D | THR261 | |
| A | PHE122 | |
| D | ARG272 | |
| E | GLY98 | |
| E | PHE99 | |
| E | VAL100 | |
| E | ASP119 | |
| E | ASN120 | |
| E | PHE122 | |
| E | THR123 | |
| E | GLY124 | |
| E | ASP144 | |
| A | THR123 | |
| E | VAL145 | |
| E | LEU159 | |
| E | THR178 | |
| E | LYS235 | |
| E | THR261 | |
| E | ARG272 | |
| F | GLY98 | |
| F | PHE99 | |
| F | VAL100 | |
| F | ASP119 | |
| A | GLY124 | |
| F | ASN120 | |
| F | PHE122 | |
| F | THR123 | |
| F | GLY124 | |
| F | ASP144 | |
| F | VAL145 | |
| F | LEU159 | |
| F | THR178 | |
| F | LYS235 | |
| F | THR261 | |
| A | ASP144 | |
| F | ARG272 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4LK3 |
| Chain | Residue | Details |
| A | LEU149 | |
| A | GLN248 | |
| A | GLU249 | |
| B | LEU149 | |
| B | TYR150 | |
| B | LYS177 | |
| B | ASN185 | |
| B | GLY188 | |
| B | LYS191 | |
| B | ARG192 | |
| B | ALA200 | |
| A | TYR150 | |
| B | TYR245 | |
| B | GLN248 | |
| B | GLU249 | |
| C | LEU149 | |
| C | TYR150 | |
| C | LYS177 | |
| C | ASN185 | |
| C | GLY188 | |
| C | LYS191 | |
| C | ARG192 | |
| A | LYS177 | |
| C | ALA200 | |
| C | TYR245 | |
| C | GLN248 | |
| C | GLU249 | |
| D | LEU149 | |
| D | TYR150 | |
| D | LYS177 | |
| D | ASN185 | |
| D | GLY188 | |
| D | LYS191 | |
| A | ASN185 | |
| D | ARG192 | |
| D | ALA200 | |
| D | TYR245 | |
| D | GLN248 | |
| D | GLU249 | |
| E | LEU149 | |
| E | TYR150 | |
| E | LYS177 | |
| E | ASN185 | |
| E | GLY188 | |
| A | GLY188 | |
| E | LYS191 | |
| E | ARG192 | |
| E | ALA200 | |
| E | TYR245 | |
| E | GLN248 | |
| E | GLU249 | |
| F | LEU149 | |
| F | TYR150 | |
| F | LYS177 | |
| F | ASN185 | |
| A | LYS191 | |
| F | GLY188 | |
| F | LYS191 | |
| F | ARG192 | |
| F | ALA200 | |
| F | TYR245 | |
| F | GLN248 | |
| F | GLU249 | |
| A | ARG192 | |
| A | ALA200 | |
| A | TYR245 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4M55 |
| Chain | Residue | Details |
| A | SER161 | |
| B | SER161 | |
| C | SER161 | |
| D | SER161 | |
| E | SER161 | |
| F | SER161 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22810237, ECO:0007744|PDB:2B69 |
| Chain | Residue | Details |
| A | TYR231 | |
| B | TYR231 | |
| C | TYR231 | |
| D | TYR231 | |
| E | TYR231 | |
| F | TYR231 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4LK3, ECO:0007744|PDB:4M55 |
| Chain | Residue | Details |
| A | HIS267 | |
| B | HIS267 | |
| C | HIS267 | |
| D | HIS267 | |
| E | HIS267 | |
| F | HIS267 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR94 | |
| B | THR94 | |
| C | THR94 | |
| D | THR94 | |
| E | THR94 | |
| F | THR94 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN316 | |
| B | ASN316 | |
| C | ASN316 | |
| D | ASN316 | |
| E | ASN316 | |
| F | ASN316 |
