3PM9
Crystal structure of a Putative dehydrogenase (RPA1076) from Rhodopseudomonas palustris CGA009 at 2.57 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0022904 | biological_process | respiratory electron transport chain |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0071949 | molecular_function | FAD binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0022904 | biological_process | respiratory electron transport chain |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD A 476 |
| Chain | Residue |
| A | PRO79 |
| A | GLN90 |
| A | LEU101 |
| A | ALA121 |
| A | LEU143 |
| A | GLY144 |
| A | ALA145 |
| A | CYS149 |
| A | THR150 |
| A | GLY153 |
| A | ASN154 |
| A | GLN80 |
| A | SER156 |
| A | THR157 |
| A | ALA159 |
| A | GLY160 |
| A | GLU210 |
| A | GLY211 |
| A | GLY214 |
| A | ILE215 |
| A | ILE216 |
| A | GLU433 |
| A | GLY81 |
| A | ASN470 |
| A | HOH533 |
| A | HOH632 |
| A | HOH686 |
| A | HOH979 |
| A | GLY82 |
| A | ASN83 |
| A | THR84 |
| A | GLY85 |
| A | LEU86 |
| A | GLY89 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 478 |
| Chain | Residue |
| A | THR60 |
| A | ARG108 |
| A | GLU178 |
| A | HOH849 |
| A | HOH1414 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 484 |
| Chain | Residue |
| A | LYS352 |
| A | HIS353 |
| A | ASP354 |
| A | HIS434 |
| A | LYS440 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 490 |
| Chain | Residue |
| A | SER341 |
| A | GLN344 |
| A | LYS352 |
| A | PHE385 |
| A | HIS394 |
| A | ASN396 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD B 476 |
| Chain | Residue |
| B | GLU43 |
| B | PRO79 |
| B | GLN80 |
| B | GLY81 |
| B | GLY82 |
| B | ASN83 |
| B | THR84 |
| B | GLY85 |
| B | GLY89 |
| B | GLN90 |
| B | LEU101 |
| B | ALA121 |
| B | ALA145 |
| B | CYS149 |
| B | THR150 |
| B | GLY152 |
| B | GLY153 |
| B | ASN154 |
| B | SER156 |
| B | THR157 |
| B | ALA159 |
| B | GLY160 |
| B | GLU210 |
| B | GLY211 |
| B | GLY214 |
| B | ILE216 |
| B | GLU433 |
| B | ASN470 |
| B | HOH523 |
| B | HOH542 |
| B | HOH766 |
| B | HOH810 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 479 |
| Chain | Residue |
| B | THR60 |
| B | ARG108 |
| B | GLU178 |
| B | HOH1130 |
| B | HOH1172 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 485 |
| Chain | Residue |
| B | ASP354 |
| B | HIS434 |
| B | LYS440 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 491 |
| Chain | Residue |
| B | SER341 |
| B | GLN344 |
| B | LYS352 |
| B | PHE385 |
| B | ASN396 |
| site_id | AC9 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD C 476 |
| Chain | Residue |
| C | ASN83 |
| C | THR84 |
| C | GLY85 |
| C | LEU86 |
| C | GLY89 |
| C | GLN90 |
| C | LEU101 |
| C | LEU143 |
| C | GLY144 |
| C | ALA145 |
| C | CYS149 |
| C | THR150 |
| C | GLY152 |
| C | GLY153 |
| C | ASN154 |
| C | SER156 |
| C | THR157 |
| C | ALA159 |
| C | GLY160 |
| C | GLU210 |
| C | GLY211 |
| C | GLY214 |
| C | ILE216 |
| C | GLU433 |
| C | ASN470 |
| C | HOH760 |
| C | HOH785 |
| C | HOH1195 |
| C | HOH1230 |
| C | PRO79 |
| C | GLN80 |
| C | GLY81 |
| C | GLY82 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 480 |
| Chain | Residue |
| C | THR60 |
| C | ARG108 |
| C | GLU178 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 486 |
| Chain | Residue |
| C | LYS352 |
| C | ASP354 |
| C | HIS434 |
| C | LYS440 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 492 |
| Chain | Residue |
| C | SER341 |
| C | GLN344 |
| C | LYS352 |
| C | PHE385 |
| C | ASN396 |
| site_id | BC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD D 476 |
| Chain | Residue |
| D | PRO79 |
| D | GLN80 |
| D | GLY81 |
| D | GLY82 |
| D | ASN83 |
| D | THR84 |
| D | GLY85 |
| D | GLY89 |
| D | GLN90 |
| D | LEU101 |
| D | ALA121 |
| D | LEU143 |
| D | GLY144 |
| D | ALA145 |
| D | CYS149 |
| D | THR150 |
| D | GLY152 |
| D | GLY153 |
| D | ASN154 |
| D | SER156 |
| D | THR157 |
| D | ALA159 |
| D | GLY160 |
| D | GLU210 |
| D | GLY211 |
| D | GLY214 |
| D | ILE216 |
| D | GLU433 |
| D | ASN470 |
| D | HOH521 |
| D | HOH629 |
| D | HOH692 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 D 481 |
| Chain | Residue |
| D | THR60 |
| D | ARG108 |
| D | GLU178 |
| D | HOH696 |
| D | HOH1294 |
| D | HOH1300 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 D 487 |
| Chain | Residue |
| D | LYS352 |
| D | HIS353 |
| D | ASP354 |
| D | HIS434 |
| D | LYS440 |
| D | HOH878 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 D 493 |
| Chain | Residue |
| D | SER341 |
| D | GLN344 |
| D | LYS352 |
| D | PHE385 |
| D | HIS394 |
| D | ASN396 |
| site_id | BC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD E 476 |
| Chain | Residue |
| E | PRO79 |
| E | GLN80 |
| E | GLY81 |
| E | GLY82 |
| E | ASN83 |
| E | THR84 |
| E | GLY85 |
| E | LEU86 |
| E | GLY89 |
| E | GLN90 |
| E | LEU101 |
| E | ALA121 |
| E | LEU143 |
| E | GLY144 |
| E | ALA145 |
| E | CYS149 |
| E | THR150 |
| E | GLY152 |
| E | GLY153 |
| E | ASN154 |
| E | SER156 |
| E | THR157 |
| E | ALA159 |
| E | GLY160 |
| E | GLU210 |
| E | GLY211 |
| E | GLY214 |
| E | ILE215 |
| E | ILE216 |
| E | GLU433 |
| E | ASN470 |
| E | HOH562 |
| E | HOH573 |
| E | HOH601 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 E 482 |
| Chain | Residue |
| E | THR60 |
| E | ARG108 |
| E | GLU178 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 E 488 |
| Chain | Residue |
| E | HIS353 |
| E | ASP354 |
| E | HIS434 |
| E | LYS440 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 E 494 |
| Chain | Residue |
| E | SER341 |
| E | GLN344 |
| E | LYS352 |
| E | PHE385 |
| E | HIS394 |
| E | ASN396 |
| site_id | CC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD F 476 |
| Chain | Residue |
| F | PRO79 |
| F | GLN80 |
| F | GLY81 |
| F | GLY82 |
| F | ASN83 |
| F | THR84 |
| F | GLY85 |
| F | GLY89 |
| F | GLN90 |
| F | LEU101 |
| F | ALA121 |
| F | LEU143 |
| F | GLY144 |
| F | ALA145 |
| F | CYS149 |
| F | THR150 |
| F | GLY153 |
| F | ASN154 |
| F | SER156 |
| F | THR157 |
| F | ALA159 |
| F | GLY160 |
| F | GLU210 |
| F | GLY211 |
| F | GLY214 |
| F | ILE215 |
| F | ILE216 |
| F | GLU433 |
| F | ASN470 |
| F | HOH569 |
| F | HOH775 |
| F | HOH1413 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 F 483 |
| Chain | Residue |
| F | THR60 |
| F | ARG108 |
| F | GLU178 |
| F | HOH1017 |
| F | HOH1270 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 F 489 |
| Chain | Residue |
| F | LYS352 |
| F | ASP354 |
| F | HIS434 |
| F | LYS440 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 F 495 |
| Chain | Residue |
| F | SER341 |
| F | GLN344 |
| F | LYS352 |
| F | PHE385 |
| F | ASN396 |
