Structure of PDB 1rqx Chain A

Receptor sequence

>1rqxA (length=331) Species: 74568 (Pseudomonas sp. ACP)

MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGN
KTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQE
NWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYA
IPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMV
VGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLERDIMRADV
VLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVR
NGEFPEGSRVLYAHLGGVPALNGYSFIFRDG

3D structure

• PDB: 1rqx Structural analysis of 1-aminocyclopropane-1-carboxylate deaminase: observation of an aminyl intermediate and identification of Tyr 294 as the active-site nucleophile.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K51 Y268 Y294
• Catalytic site (residue number reindexed from 1): K51 Y261 Y287
• Enzyme Commision number: 3.5.99.7: 1-aminocyclopropane-1-carboxylate deaminase.

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	PLP	A	N50 K51 K54 N79 S197 T199 G200 T202 Y294 E295 L322 G323 G324	N50 K51 K54 N79 S190 T192 G193 T195 Y287 E288 L315 G316 G317
BS02	MLP	A	K51 S78 N79 Q80 Y294	K51 S78 N79 Q80 Y287

Gene Ontology

Molecular Function

• GO:0008660 1-aminocyclopropane-1-carboxylate deaminase activity
• GO:0016787 hydrolase activity
• GO:0019148 D-cysteine desulfhydrase activity
• GO:0030170 pyridoxal phosphate binding

Biological Process

• GO:0009310 amine catabolic process
• GO:0018871 1-aminocyclopropane-1-carboxylate metabolic process

External links

• PDB: RCSB:1rqx, PDBe:1rqx, PDBj:1rqx
• PDBsum: 1rqx
• PubMed: 15221829
• UniProt: Q00740|1A1D_PSEUD 1-aminocyclopropane-1-carboxylate deaminase (Gene Name=acdS)