Structure of PDB 1q19 Chain D

Receptor sequence
>1q19D (length=500) Species: 554 (Pectobacterium carotovorum) [Search protein sequence]
SNSFCVVYKGSDTDINNIQRDFDGKGEALSNGYLFIEQNGHYQKCEMERG
TAYLIGSLYNRTFLIGLAGVWEGEAYLANDAELLALLFTRLGANALALAE
GDFCFFIDEPNGELTVITESRGFSPVHVVQGKKAWMTNSLKLVTAAEGEG
ALWFEEEALVCQSLMRADTYTPVKNAQRLKPGAVHVLTHDSEGYSFVESR
TLTTPASNQLLALPREPLLALIDRYLNAPLEDLAPRFDTVGIPLSGGLDS
SLVTALASRHFKKLNTYSIGTELSNEFEFSQQVADALGTHHQMKILSETE
VINGIIESIYYNEIFDGLSAEIQSGLFNVYRQAQGQVSCMLTGYGSDLLF
GGILKPGAQYDNPNQLLAEQVYRTRWTGEFATHGASCYGIDIRHPFWSHS
LISLCHALHPDYKIFDNEVKNILREYADSLQLLPKDIVWRKKIGIHEGSS
VNQAFANVLGSTVDNYQTKSRFTYRVYQAFLRGRLSITDVTPSQLKDLIK
3D structure
PDB1q19 Crystal Structure of Carbapenam Synthetase (CarA)
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G57 L319 E322 Y345 E380 K443
Catalytic site (residue number reindexed from 1) G56 L318 E321 Y344 E379 K442
Enzyme Commision number 6.3.3.6: carbapenam-3-carboxylate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 APC D P244 L245 S246 G248 D250 S251 S269 I270 T343 G344 D348 K443 I444 G445 I446 P243 L244 S245 G247 D249 S250 S268 I269 T342 G343 D347 K442 I443 G444 I445
BS02 SSC D I323 Y345 G346 D348 I322 Y344 G345 D347
Gene Ontology
Molecular Function
GO:0004066 asparagine synthase (glutamine-hydrolyzing) activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006529 asparagine biosynthetic process
GO:0017000 antibiotic biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q19, PDBe:1q19, PDBj:1q19
PDBsum1q19
PubMed12890666
UniProtQ9XB61|CARA_PECCC Carbapenam-3-carboxylate synthase (Gene Name=carA)

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