Structure of PDB 1f2d Chain D

Receptor sequence
>1f2dD (length=341) [Search protein sequence]
AGVAKFAKYPLTFGPSPISNLNRLSQHLGSKVNVYAKREDCNSGLAFGGN
KLRKLEYIVPDIVEGDYTHLVSIGGRQSNQTRMVAALAAKLGKKCVLIQE
DWVPIPEAEKDVYNRVGNIELSRIMGADVRVIEDGFDIGMRKSFANALQE
LEDAGHKPYPIPAGCSEHKYGGLGFVGFADEVINQEVELGIKFDKIVVCC
VTGSTTAGILAGMAQYGRQDDVIAIDASFTSEKTKEQTLRIANNTAKLIG
VEHEFKDFTLDTRFAYPCYGVPNEGTIEAIRTCAEQEGVLTDPVYEGKSM
QGLIALIKEDYFKPGANVLYVHLGGAPALSAYSSFFPTKTA
3D structure
PDB1f2d Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus.
ChainD
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 Y269 Y295
Catalytic site (residue number reindexed from 1) K51 Y269 Y295
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 D N50 K51 K54 N79 C200 T202 G203 T205 Y295 E296 L323 G324 G325 N50 K51 K54 N79 C200 T202 G203 T205 Y295 E296 L323 G324 G325
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1f2d, PDBe:1f2d, PDBj:1f2d
PDBsum1f2d
PubMed10938279
UniProtQ7M523|1A1D_CYBSA 1-aminocyclopropane-1-carboxylate deaminase

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