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 | 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 | 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 | 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 | 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 | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q8ZNF3 |
Chain | Residue | Details |
A | LYS186 | |
B | LYS186 | |
C | LYS186 | |
D | LYS186 |