2PLS
Structural Genomics, the crystal structure of the CorC/HlyC transporter associated domain of a CBS domain protein from Chlorobium tepidum TLS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
L | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 904 |
Chain | Residue |
A | HOH934 |
B | HOH814 |
B | HOH834 |
C | HOH839 |
C | HOH842 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT D 902 |
Chain | Residue |
F | HOH782 |
D | HOH913 |
D | HOH924 |
D | HOH925 |
F | HOH769 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT E 903 |
Chain | Residue |
D | LEU392 |
E | LEU392 |
E | HOH917 |
F | LEU392 |
F | HOH729 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG G 603 |
Chain | Residue |
G | ASP413 |
G | ASP415 |
G | HOH650 |
H | ASP420 |
H | HOH617 |
H | HOH622 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG H 601 |
Chain | Residue |
G | ASP420 |
G | HOH614 |
G | HOH644 |
H | ASP413 |
H | ASP415 |
H | MG602 |
H | HOH623 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG H 602 |
Chain | Residue |
G | ASP413 |
G | ASP415 |
G | ASP420 |
H | ASP413 |
H | ASP415 |
H | ASP420 |
H | MG601 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG I 605 |
Chain | Residue |
I | ASP413 |
I | ASP415 |
I | ASP420 |
I | MG606 |
J | ASP413 |
J | ASP415 |
J | ASP420 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG I 606 |
Chain | Residue |
I | ASP413 |
I | ASP415 |
I | MG605 |
J | ASP420 |
J | HOH764 |
J | HOH765 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG J 604 |
Chain | Residue |
I | ASP420 |
I | HOH841 |
J | ASP413 |
J | ASP415 |
J | HOH762 |
J | HOH763 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT K 901 |
Chain | Residue |
K | ASP413 |
K | MSE414 |
K | ASP420 |
K | HOH942 |
L | ASP415 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 706 |
Chain | Residue |
A | GLU375 |
A | GLY379 |
A | VAL380 |
A | TYR381 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 712 |
Chain | Residue |
A | GLN397 |
A | THR398 |
A | HOH907 |
C | VAL373 |
C | GLU376 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 702 |
Chain | Residue |
B | GLU375 |
B | GLU377 |
B | GLY379 |
B | VAL380 |
B | TYR381 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 703 |
Chain | Residue |
C | GLU375 |
C | GLY379 |
C | VAL380 |
C | TYR381 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 709 |
Chain | Residue |
B | VAL373 |
B | GLU376 |
C | GLN397 |
C | THR398 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 714 |
Chain | Residue |
C | ALA360 |
C | PRO362 |
C | GLU363 |
C | HOH860 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 704 |
Chain | Residue |
D | PHE403 |
D | HOH913 |
E | LEU392 |
E | ASP400 |
E | ILE401 |
E | HOH943 |
E | HOH953 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO E 705 |
Chain | Residue |
E | GLU375 |
E | GLY379 |
E | VAL380 |
E | TYR381 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F 701 |
Chain | Residue |
F | TYR381 |
F | HOH719 |
F | GLU375 |
F | GLY379 |
F | VAL380 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO F 710 |
Chain | Residue |
F | GLN347 |
F | TRP353 |
F | THR367 |
F | LEU368 |
F | GLY369 |
F | TRP407 |
F | LYS426 |
F | HOH755 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F 713 |
Chain | Residue |
D | ARG394 |
F | TRP390 |
F | LEU391 |
F | HOH729 |
F | HOH767 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO I 708 |
Chain | Residue |
I | GLU375 |
I | GLY379 |
I | VAL380 |
I | TYR381 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO J 711 |
Chain | Residue |
J | ASP350 |
J | GLY351 |
J | SER352 |
J | THR425 |
J | LYS426 |
J | HOH714 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 804 |
Chain | Residue |
B | ASP428 |
C | ARG408 |
C | GLU410 |
K | ASP366 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT C 802 |
Chain | Residue |
C | GLU410 |
C | VAL411 |
C | ILE412 |
K | HOH916 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT D 803 |
Chain | Residue |
D | GLN347 |
D | ARG348 |
D | GLU349 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT I 801 |
Chain | Residue |
I | ARG348 |
I | ASP350 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT I 805 |
Chain | Residue |
A | ARG371 |
I | LEU368 |
I | GLY369 |
I | GLU405 |
I | TRP407 |
I | LYS426 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT L 806 |
Chain | Residue |
L | ASP350 |
L | GLY351 |
L | SER352 |
L | THR425 |
L | LYS426 |