Structure of PDB 1tyz Chain A

Receptor sequence
>1tyzA (length=331) Species: 74568 (Pseudomonas sp. ACP) [Search protein sequence]
MNLQRFPRYPLTFGPTPIQPLARLSKHLGGKVHLYAKREDCNSGLAFGGN
KTRKLEYLIPEALAQGCDTLVSIGGIQSNQTRQVAAVAAHLGMKCVLVQE
NWVNYSDAVYDRVGNIQMSRILGADVRLVPDRSWEDALESVRAAGGKPYA
IPAGCSDHPLGGLGFVGFAEEVRAQEAELGFKFDYVVVCSVTGSTQAGMV
VGFAADGRADRVIGVDASAKPAQTREQITRIARQTAEKVGLERDIMRADV
VLDERFAGPEYGLPNEGTLEAIRLCARTEGMLTDPVYEGKSMHGMIEMVR
NGEFPEGSRVLYAHLGGVPALNGYSFIFRDG
3D structure
PDB1tyz Structural Analysis of Pseudomonas 1-Aminocyclopropane-1-carboxylate Deaminase Complexes:Insight into the mechanism of unique pyrodoxial-5'-phosphate dependent cyclopropane ring opening reaction
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C196 S197 T199 G200 T202 Y294 E295 L322 G323 G324 N50 K51 K54 N79 C189 S190 T192 G193 T195 Y287 E288 L315 G316 G317
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1tyz, PDBe:1tyz, PDBj:1tyz
PDBsum1tyz
PubMed15491139
UniProtQ00740|1A1D_PSEUD 1-aminocyclopropane-1-carboxylate deaminase (Gene Name=acdS)

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