Structure of PDB 1kbp Chain D

Receptor sequence
>1kbpD (length=424) Species: 3885 (Phaseolus vulgaris) [Search protein sequence]
RDMPLDSDVFRVPPGYNAPQQVHITQGDLVGRAMIISWVTMDEPGSSAVR
YWSEKNGRKRIAKGKMSTYRFFNYSSGFIHHTTIRKLKYNTKYYYEVGLR
NTTRRFSFITPPQTGLDVPYTFGLIGDLGQSFDSNTTLSHYELSPKKGQT
VLFVGDLSYADRYPNHDNVRWDTWGRFTERSVAYQPWIWTAGNHEIEFAP
EINETEPFKPFSYRYHVPYEASQSTSPFWYSIKRASAHIIVLSSYSAYGR
GTPQYTWLKKELRKVKRSETPWLIVLMHSPLYNSYNHHFMEGEAMRTKFE
AWFVKYKVDVVFAGHVHAYERSERVSNIAYKITDGLCTPVKDQSAPVYIT
IGDAGNYGVIDSNMIQPQPEYSAFREASFGHGMFDIKNRTHAHFSWNRNQ
DGVAVEADSVWFFNRHWYPVDDST
3D structure
PDB1kbp Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures.
ChainD
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D135 D164 Y167 N201 H202 H286 H295 H296 H323 H325
Catalytic site (residue number reindexed from 1) D127 D156 Y159 N193 H194 H278 H287 H288 H315 H317
Enzyme Commision number 3.1.3.2: acid phosphatase.
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 FE D D135 D164 Y167 H325 D127 D156 Y159 H317
BS02 ZN D D164 N201 H286 H323 D156 N193 H278 H315
Gene Ontology
Molecular Function
GO:0003993 acid phosphatase activity
GO:0008199 ferric iron binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1kbp, PDBe:1kbp, PDBj:1kbp
PDBsum1kbp
PubMed8683579
UniProtP80366|PPAF_PHAVU Fe(3+)-Zn(2+) purple acid phosphatase

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