6VO6
Crystal Structure of Cj1427, an Essential NAD-dependent Dehydrogenase from Campylobacter jejuni, in the Presence of NADH and GDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019003 | molecular_function | GDP binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
A | 0051289 | biological_process | protein homotetramerization |
A | 0070404 | molecular_function | NADH binding |
B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019003 | molecular_function | GDP binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
B | 0051289 | biological_process | protein homotetramerization |
B | 0070404 | molecular_function | NADH binding |
C | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019003 | molecular_function | GDP binding |
C | 0042802 | molecular_function | identical protein binding |
C | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
C | 0051289 | biological_process | protein homotetramerization |
C | 0070404 | molecular_function | NADH binding |
D | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019003 | molecular_function | GDP binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0045227 | biological_process | capsule polysaccharide biosynthetic process |
D | 0051289 | biological_process | protein homotetramerization |
D | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | binding site for residue NAI A 401 |
Chain | Residue |
A | GLY9 |
A | GLY56 |
A | ASP57 |
A | ALA58 |
A | LEU77 |
A | ALA78 |
A | ALA79 |
A | VAL81 |
A | ILE96 |
A | PRO117 |
A | ASN118 |
A | ALA11 |
A | TYR144 |
A | LYS148 |
A | LEU166 |
A | VAL169 |
A | ARG175 |
A | ARG177 |
A | LEU180 |
A | EDO403 |
A | HOH533 |
A | HOH548 |
A | GLY12 |
A | HOH595 |
A | HOH615 |
C | ASN311 |
A | TYR13 |
A | ILE14 |
A | ASP33 |
A | ASN34 |
A | MET36 |
A | GLN39 |
site_id | AC2 |
Number of Residues | 25 |
Details | binding site for residue GDP A 402 |
Chain | Residue |
A | GLY82 |
A | PRO84 |
A | THR168 |
A | ASP179 |
A | LEU180 |
A | LEU181 |
A | ASP184 |
A | PHE185 |
A | VAL196 |
A | LEU197 |
A | PHE198 |
A | ARG204 |
A | LYS242 |
A | ARG270 |
A | HOH533 |
A | HOH535 |
A | HOH543 |
A | HOH560 |
A | HOH561 |
A | HOH600 |
A | HOH673 |
A | HOH678 |
A | HOH687 |
A | HOH708 |
C | PHE194 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | THR119 |
A | ASN120 |
A | SER121 |
A | LEU166 |
A | ALA167 |
A | THR168 |
A | ARG270 |
A | TYR272 |
A | NAI401 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | THR52 |
A | GLU67 |
A | LYS70 |
A | EDO405 |
A | HOH503 |
A | HOH627 |
A | HOH652 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | LYS4 |
A | VAL5 |
A | GLU28 |
A | CYS30 |
A | LYS70 |
A | EDO404 |
A | HOH532 |
A | HOH544 |
A | HOH627 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | ASN62 |
A | ARG65 |
A | HOH504 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CL A 407 |
Chain | Residue |
A | SER237 |
A | THR289 |
A | LEU290 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue TMA A 408 |
Chain | Residue |
A | ALA69 |
A | LYS70 |
A | ALA71 |
A | ASP72 |
A | HOH731 |
site_id | AC9 |
Number of Residues | 34 |
Details | binding site for residue NAI B 401 |
Chain | Residue |
B | ASN34 |
B | MET36 |
B | PHE37 |
B | GLN39 |
B | GLY56 |
B | ASP57 |
B | ALA58 |
B | LEU77 |
B | ALA78 |
B | ALA79 |
B | VAL81 |
B | ILE96 |
B | PRO117 |
B | ASN118 |
B | TYR144 |
B | LYS148 |
B | LEU166 |
B | VAL169 |
B | ARG175 |
B | ARG177 |
B | LEU180 |
B | EDO403 |
B | HOH540 |
B | HOH583 |
B | HOH616 |
B | HOH622 |
B | HOH670 |
D | ASN311 |
B | GLY9 |
B | ALA11 |
B | GLY12 |
B | TYR13 |
B | ILE14 |
B | ASP33 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | LEU23 |
B | ASN48 |
B | HOH518 |
B | HOH610 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | VAL81 |
B | TYR144 |
B | ARG177 |
B | NAI401 |
B | HOH540 |
B | HOH558 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
A | GLU247 |
A | LYS251 |
A | HOH520 |
B | PRO110 |
B | SER111 |
B | HOH506 |
B | HOH576 |
B | HOH587 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | LYS242 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue TMA B 406 |
Chain | Residue |
B | ASP287 |
B | ASN288 |
B | ASP292 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue TMA B 407 |
Chain | Residue |
B | PHE198 |
D | GLU135 |
D | LYS193 |
D | ASP255 |
D | HOH804 |
site_id | AD7 |
Number of Residues | 34 |
Details | binding site for residue NAI C 401 |
Chain | Residue |
A | ASN311 |
C | GLY9 |
C | ALA11 |
C | GLY12 |
C | TYR13 |
C | ILE14 |
C | ASP33 |
C | ASN34 |
C | MET36 |
C | PHE37 |
C | GLN39 |
C | GLY56 |
C | ASP57 |
C | ALA58 |
C | LEU77 |
C | ALA78 |
C | ALA79 |
C | VAL81 |
C | ILE96 |
C | PRO117 |
C | ASN118 |
C | TYR144 |
C | LYS148 |
C | LEU166 |
C | VAL169 |
C | ARG175 |
C | ARG177 |
C | LEU180 |
C | EDO403 |
C | HOH530 |
C | HOH570 |
C | HOH581 |
C | HOH609 |
C | HOH678 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue EDO C 402 |
Chain | Residue |
C | THR52 |
C | GLU67 |
C | LYS70 |
C | HOH520 |
C | HOH555 |
C | HOH569 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue EDO C 403 |
Chain | Residue |
C | VAL81 |
C | TYR144 |
C | ARG177 |
C | NAI401 |
C | HOH526 |
C | HOH560 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue EDO C 404 |
Chain | Residue |
C | LYS4 |
C | VAL5 |
C | GLU28 |
C | CYS30 |
C | LYS70 |
C | HOH502 |
C | HOH555 |
C | HOH557 |
C | HOH613 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue TMA C 405 |
Chain | Residue |
C | ALA69 |
C | LYS70 |
C | ALA71 |
C | ASP72 |
site_id | AE3 |
Number of Residues | 32 |
Details | binding site for residue NAI D 401 |
Chain | Residue |
B | ASN311 |
B | HOH551 |
D | GLY9 |
D | ALA11 |
D | GLY12 |
D | TYR13 |
D | ILE14 |
D | ASP33 |
D | ASN34 |
D | MET36 |
D | GLN39 |
D | GLY56 |
D | ASP57 |
D | ALA58 |
D | LEU77 |
D | ALA78 |
D | ALA79 |
D | VAL81 |
D | ILE96 |
D | PRO117 |
D | ASN118 |
D | TYR144 |
D | LYS148 |
D | LEU166 |
D | VAL169 |
D | ARG175 |
D | ARG177 |
D | LEU180 |
D | EDO404 |
D | HOH548 |
D | HOH600 |
D | HOH606 |
site_id | AE4 |
Number of Residues | 22 |
Details | binding site for residue GDP D 402 |
Chain | Residue |
D | GLY82 |
D | THR168 |
D | ASP179 |
D | LEU180 |
D | LEU181 |
D | ASP184 |
D | PHE185 |
D | VAL196 |
D | LEU197 |
D | PHE198 |
D | ARG204 |
D | LYS242 |
D | ARG270 |
D | HOH501 |
D | HOH530 |
D | HOH548 |
D | HOH582 |
D | HOH647 |
D | HOH660 |
D | HOH664 |
D | HOH686 |
D | HOH699 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue NA D 403 |
Chain | Residue |
D | GLY124 |
D | GLU127 |
D | ASP271 |
D | HOH605 |
D | HOH662 |
site_id | AE6 |
Number of Residues | 9 |
Details | binding site for residue EDO D 404 |
Chain | Residue |
D | THR119 |
D | ASN120 |
D | SER121 |
D | LEU166 |
D | ALA167 |
D | THR168 |
D | ARG270 |
D | TYR272 |
D | NAI401 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue EDO D 405 |
Chain | Residue |
D | THR52 |
D | GLU67 |
D | LYS70 |
D | HOH517 |
D | HOH519 |
D | HOH651 |
site_id | AE8 |
Number of Residues | 3 |
Details | binding site for residue TMA D 406 |
Chain | Residue |
D | ASP287 |
D | ASN288 |
D | ASP292 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32168450, ECO:0007744|PDB:6VO6 |
Chain | Residue | Details |
B | TYR144 | |
B | THR168 | |
B | VAL169 | |
B | ARG175 | |
B | ASP179 | |
B | VAL196 | |
B | ARG204 | |
B | LYS242 | |
B | ARG270 | |
B | ASN311 | |
C | TYR13 | |
C | ASP33 | |
C | PHE37 | |
C | ASP57 | |
C | LEU77 | |
C | TYR144 | |
C | THR168 | |
C | VAL169 | |
C | ARG175 | |
C | ASP179 | |
C | VAL196 | |
C | ARG204 | |
C | LYS242 | |
C | ARG270 | |
C | ASN311 | |
D | TYR13 | |
D | ASP33 | |
D | PHE37 | |
D | ASP57 | |
D | LEU77 | |
D | TYR144 | |
D | THR168 | |
D | VAL169 | |
D | ARG175 | |
D | ASP179 | |
D | VAL196 | |
D | ARG204 | |
D | LYS242 | |
D | ARG270 | |
D | ASN311 | |
A | TYR13 | |
A | ASP33 | |
A | PHE37 | |
A | ASP57 | |
A | LEU77 | |
A | TYR144 | |
A | THR168 | |
A | VAL169 | |
A | ARG175 | |
A | ASP179 | |
A | VAL196 | |
A | ARG204 | |
A | LYS242 | |
A | ARG270 | |
A | ASN311 | |
B | TYR13 | |
B | ASP33 | |
B | PHE37 | |
B | ASP57 | |
B | LEU77 |