Structure of PDB 1f2d Chain B

Receptor sequence
>1f2dB (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.
ChainB
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 B K51 K54 N79 C200 T202 G203 T205 Y295 E296 L323 G324 G325 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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