3R4I
Crystal structure of a Citrate lyase (Bxe_B2899) from BURKHOLDERIA XENOVORANS LB400 at 2.24 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
A | 0106064 | biological_process | regulation of cobalamin metabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
B | 0106064 | biological_process | regulation of cobalamin metabolic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
C | 0106064 | biological_process | regulation of cobalamin metabolic process |
D | 0003824 | molecular_function | catalytic activity |
D | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
D | 0106064 | biological_process | regulation of cobalamin metabolic process |
E | 0003824 | molecular_function | catalytic activity |
E | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
E | 0016829 | molecular_function | lyase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
E | 0106064 | biological_process | regulation of cobalamin metabolic process |
F | 0003824 | molecular_function | catalytic activity |
F | 0008815 | molecular_function | citrate (pro-3S)-lyase activity |
F | 0016829 | molecular_function | lyase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0047777 | molecular_function | (S)-citramalyl-CoA lyase activity |
F | 0106064 | biological_process | regulation of cobalamin metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 341 |
Chain | Residue |
A | GLU151 |
A | ASP177 |
A | HOH372 |
A | HOH381 |
A | HOH427 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 346 |
Chain | Residue |
B | HOH408 |
A | ASP230 |
A | HOH390 |
A | HOH391 |
A | HOH550 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 339 |
Chain | Residue |
B | GLU151 |
B | ASP177 |
B | CL354 |
B | HOH395 |
B | HOH397 |
B | HOH432 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 340 |
Chain | Residue |
A | HOH385 |
A | HOH561 |
B | ASP230 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 354 |
Chain | Residue |
B | GLY174 |
B | LEU175 |
B | MSE176 |
B | ASP177 |
B | CA339 |
B | HOH483 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 343 |
Chain | Residue |
C | ARG86 |
C | GLU151 |
C | ASP177 |
C | CL353 |
C | HOH407 |
C | HOH442 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 344 |
Chain | Residue |
C | ASP230 |
C | HOH402 |
C | HOH426 |
D | HOH388 |
D | HOH409 |
D | HOH439 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL C 353 |
Chain | Residue |
C | GLY174 |
C | LEU175 |
C | MSE176 |
C | ASP177 |
C | ALA300 |
C | CA343 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT C 357 |
Chain | Residue |
C | ARG86 |
C | MSE176 |
C | TRP251 |
C | ILE253 |
C | ASP298 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 342 |
Chain | Residue |
D | GLU151 |
D | ASP177 |
D | CL352 |
D | HOH364 |
D | HOH430 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 345 |
Chain | Residue |
C | HOH382 |
C | HOH404 |
C | HOH446 |
D | ASP230 |
D | HOH549 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA D 350 |
Chain | Residue |
C | ASP91 |
C | HIS120 |
D | GLU126 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL D 352 |
Chain | Residue |
D | GLY174 |
D | MSE176 |
D | ASP177 |
D | ALA300 |
D | CA342 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT D 358 |
Chain | Residue |
D | ARG86 |
D | MSE176 |
D | TRP251 |
D | ASP298 |
D | HOH364 |
D | HOH430 |
D | HOH433 |
site_id | BC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA E 347 |
Chain | Residue |
E | ASP230 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA E 348 |
Chain | Residue |
E | GLU151 |
E | ASP177 |
E | CL355 |
E | HOH463 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL E 355 |
Chain | Residue |
E | GLY174 |
E | LEU175 |
E | MSE176 |
E | ASP177 |
E | CA348 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA F 349 |
Chain | Residue |
F | ARG86 |
F | GLU151 |
F | ASP177 |
F | CL356 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA F 351 |
Chain | Residue |
E | HOH558 |
F | ASP230 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL F 356 |
Chain | Residue |
F | GLY174 |
F | MSE176 |
F | ASP177 |
F | ALA300 |
F | CA349 |