5K8B
X-ray structure of KdnA, 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase, from Shewanella oneidensis in the presence of the external aldimine with PLP and glutamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue PDG A 501 |
| Chain | Residue |
| A | SER60 |
| A | ASP183 |
| A | LYS186 |
| A | HIS325 |
| A | HOH613 |
| A | HOH645 |
| A | HOH686 |
| B | ARG222 |
| B | ASN233 |
| B | ARG235 |
| A | GLY61 |
| A | THR62 |
| A | PHE87 |
| A | VAL131 |
| A | ASP157 |
| A | CYS159 |
| A | GLN160 |
| A | SER181 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | ASN322 |
| A | TRP324 |
| A | HIS325 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | LYS262 |
| A | SER292 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue PDG B 501 |
| Chain | Residue |
| A | ARG222 |
| A | ASN233 |
| A | ARG235 |
| A | HOH636 |
| A | HOH713 |
| B | SER60 |
| B | GLY61 |
| B | THR62 |
| B | PHE87 |
| B | ASP157 |
| B | CYS159 |
| B | GLN160 |
| B | SER181 |
| B | ASP183 |
| B | LYS186 |
| B | HIS325 |
| B | HOH687 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | LYS262 |
| B | SER292 |
| B | HOH675 |
| B | HOH678 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue PDG C 501 |
| Chain | Residue |
| C | SER60 |
| C | GLY61 |
| C | THR62 |
| C | PHE87 |
| C | VAL131 |
| C | ASP157 |
| C | CYS159 |
| C | GLN160 |
| C | SER181 |
| C | ASP183 |
| C | LYS186 |
| C | HIS325 |
| C | HOH615 |
| C | HOH675 |
| D | ARG222 |
| D | ASN233 |
| D | ARG235 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | HOH634 |
| C | HOH672 |
| C | HOH729 |
| C | HOH735 |
| D | HOH762 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | LYS262 |
| C | ARG278 |
| C | PHE290 |
| C | SER292 |
| C | HOH690 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | binding site for residue PDG D 501 |
| Chain | Residue |
| C | ARG222 |
| C | ASN233 |
| C | ARG235 |
| D | SER60 |
| D | GLY61 |
| D | THR62 |
| D | PHE87 |
| D | VAL131 |
| D | ASP157 |
| D | CYS159 |
| D | GLN160 |
| D | SER181 |
| D | ASP183 |
| D | LYS186 |
| D | GLY193 |
| D | HIS325 |
| D | HOH611 |
| D | HOH644 |
| D | HOH694 |
| D | HOH713 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 502 |
| Chain | Residue |
| D | LYS262 |
| D | ARG278 |
| D | SER292 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q8ZNF3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
