2JI7
X-ray structure of Oxalyl-CoA decarboxylase with covalent reaction intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0001561 | biological_process | fatty acid alpha-oxidation |
A | 0003824 | molecular_function | catalytic activity |
A | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0033611 | biological_process | oxalate catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0043531 | molecular_function | ADP binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001561 | biological_process | fatty acid alpha-oxidation |
B | 0003824 | molecular_function | catalytic activity |
B | 0008949 | molecular_function | oxalyl-CoA decarboxylase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0033611 | biological_process | oxalate catabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0043531 | molecular_function | ADP binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 51 |
Details | BINDING SITE FOR RESIDUE OXT B1566 |
Chain | Residue |
A | VAL32 |
B | THR265 |
B | ARG266 |
B | ALA267 |
B | TRP285 |
B | LEU286 |
B | ASN358 |
B | LYS359 |
B | LEU362 |
B | TYR377 |
B | GLY400 |
A | GLU56 |
B | ALA401 |
B | ASN402 |
B | ALA403 |
B | LEU404 |
B | ASP405 |
B | ARG408 |
B | MET409 |
B | GLY426 |
B | MET428 |
B | GLY451 |
A | VAL79 |
B | ASP452 |
B | SER453 |
B | ALA454 |
B | PHE457 |
B | ASN479 |
B | GLY481 |
B | ILE482 |
B | TYR483 |
B | ARG555 |
B | MG1567 |
A | ASN86 |
B | HOH2437 |
B | HOH2457 |
B | HOH2483 |
B | HOH2559 |
B | HOH2571 |
B | HOH2572 |
B | HOH2573 |
B | HOH2574 |
B | HOH2575 |
B | HOH2576 |
A | TYR120 |
B | HOH2577 |
B | HOH2578 |
A | GLU121 |
A | HOH2032 |
B | ALA263 |
B | ALA264 |
site_id | AC2 |
Number of Residues | 53 |
Details | BINDING SITE FOR RESIDUE OXT A1566 |
Chain | Residue |
B | VAL79 |
B | ASN86 |
B | TYR120 |
B | GLU121 |
B | HOH2039 |
A | ALA263 |
A | ALA264 |
A | THR265 |
A | ARG266 |
A | ALA267 |
A | TRP285 |
A | LEU286 |
A | ASN358 |
A | LYS359 |
A | LEU362 |
A | TYR377 |
A | GLY400 |
A | ALA401 |
A | ASN402 |
A | ALA403 |
A | LEU404 |
A | ASP405 |
A | ARG408 |
A | MET409 |
A | GLY426 |
A | MET428 |
A | GLY451 |
A | ASP452 |
A | SER453 |
A | ALA454 |
A | PHE457 |
A | ASN479 |
A | GLY481 |
A | ILE482 |
A | TYR483 |
A | ARG555 |
A | MG1567 |
A | HOH2435 |
A | HOH2436 |
A | HOH2457 |
A | HOH2479 |
A | HOH2556 |
A | HOH2570 |
A | HOH2571 |
A | HOH2572 |
A | HOH2573 |
A | HOH2574 |
A | HOH2575 |
A | HOH2576 |
A | HOH2577 |
A | HOH2578 |
B | VAL32 |
B | GLU56 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B1567 |
Chain | Residue |
B | ASP452 |
B | ASN479 |
B | GLY481 |
B | OXT1566 |
B | HOH2483 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A1567 |
Chain | Residue |
A | ASP452 |
A | ASN479 |
A | GLY481 |
A | OXT1566 |
A | HOH2479 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP B1568 |
Chain | Residue |
B | ARG160 |
B | GLY221 |
B | LYS222 |
B | GLY223 |
B | TYR226 |
B | MET247 |
B | GLY280 |
B | ARG282 |
B | LEU286 |
B | ASP306 |
B | ILE307 |
B | GLY324 |
B | ASP325 |
B | ILE326 |
B | HOH2308 |
B | HOH2579 |
B | HOH2580 |
B | HOH2581 |
B | HOH2583 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP A1568 |
Chain | Residue |
A | ARG160 |
A | GLY221 |
A | LYS222 |
A | GLY223 |
A | TYR226 |
A | MET247 |
A | GLY280 |
A | ALA281 |
A | ARG282 |
A | LEU286 |
A | ASP306 |
A | ILE307 |
A | GLY324 |
A | ASP325 |
A | ILE326 |
A | HOH2266 |
A | HOH2458 |
A | HOH2580 |
A | HOH2581 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE A1569 |
Chain | Residue |
A | GLU70 |
A | ALA193 |
A | TYR226 |
A | HOH2270 |
A | HOH2583 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGE B1569 |
Chain | Residue |
B | ALA193 |
B | ALA227 |
B | GLN228 |
B | HOH2284 |
B | HOH2582 |
B | HOH2583 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE B3P A1570 |
Chain | Residue |
A | ASP489 |
A | GLY493 |
A | VAL494 |
A | ARG499 |
A | HOH2584 |
B | ASN469 |
B | LYS537 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE B3P B1570 |
Chain | Residue |
A | GLU369 |
B | MET366 |
B | THR367 |
B | GLY382 |
B | ARG385 |
B | ASP386 |
B | HOH2585 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE B3P B1571 |
Chain | Residue |
A | ASN469 |
A | HOH2474 |
B | ASP489 |
B | GLY493 |
B | VAL494 |
B | ARG499 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE B3P A1571 |
Chain | Residue |
A | MET366 |
A | THR367 |
A | GLY382 |
A | VAL383 |
A | ARG385 |
A | ASP386 |
A | HOH2398 |
A | HOH2417 |
A | HOH2420 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE B3P B1572 |
Chain | Residue |
A | LYS291 |
B | GLU109 |
B | GLU111 |
B | SER141 |
B | LYS143 |
B | ASP144 |
B | HOH2587 |
B | HOH2589 |
B | HOH2592 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE B3P A1572 |
Chain | Residue |
A | GLU109 |
A | GLU111 |
A | LYS143 |
A | ASP144 |
A | HOH2588 |
A | HOH2591 |
A | HOH2593 |
B | LYS291 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ILE34 | |
B | TYR120 | |
B | ALA263 | |
B | ALA401 | |
B | ARG408 | |
B | GLY426 | |
B | SER453 | |
B | SER553 | |
A | TYR120 | |
A | ALA263 | |
A | ALA401 | |
A | ARG408 | |
A | GLY426 | |
A | SER453 | |
A | SER553 | |
B | ILE34 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16216870, ECO:0000269|PubMed:17637344 |
Chain | Residue | Details |
A | ARG160 | |
A | TYR483 | |
B | ARG160 | |
B | LYS222 | |
B | ARG282 | |
B | ASP306 | |
B | ILE326 | |
B | TYR377 | |
B | ASP452 | |
B | ASN479 | |
B | GLY481 | |
A | LYS222 | |
B | TYR483 | |
A | ARG282 | |
A | ASP306 | |
A | ILE326 | |
A | TYR377 | |
A | ASP452 | |
A | ASN479 | |
A | GLY481 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASN358 | |
B | ASN358 |