Structure of PDB 1tyz Chain C

Receptor sequence

>1tyzC (length=338) Species: 74568 (Pseudomonas sp. ACP)

MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGN
KTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQE
NWVNYSDAVYDRVGNIQMSRILGADVRLVPDGFDIGFRRSWEDALESVRA
AGGKPYAIPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTG
STQAGMVVGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLER
DIMRADVVLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMH
GMIEMVRNGEFPEGSRVLYAHLGGVPALNGYSFIFRDG

3D structure

• PDB: 1tyz Structural Analysis of Pseudomonas 1-Aminocyclopropane-1-carboxylate Deaminase Complexes:Insight into the mechanism of unique pyrodoxial-5'-phosphate dependent cyclopropane ring opening reaction
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K51 Y268 Y294
• Catalytic site (residue number reindexed from 1): K51 Y268 Y294
• 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	C	N50 K51 K54 N79 S197 T199 G200 T202 Y294 E295 L322 G323 G324	N50 K51 K54 N79 S197 T199 G200 T202 Y294 E295 L322 G323 G324

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:1tyz, PDBe:1tyz, PDBj:1tyz
• PDBsum: 1tyz
• PubMed: 15491139
• UniProt: Q00740|1A1D_PSEUD 1-aminocyclopropane-1-carboxylate deaminase (Gene Name=acdS)