Structure of PDB 8uxx Chain B

Receptor sequence
>8uxxB (length=387) Species: 4896 (Schizosaccharomyces pombe) [Search protein sequence]
MESAPIVLDNGTGFVKVGYAKDNFPRFQFPSIVGRPILRAEEKTGNVQIK
DVMVGDEAEAVRSLLQVKYPMENGIIRDFEEMNQLWDYTFFEKLKIDPRG
RKILLTEPPMNPVANREKMCETMFERYGFGGVYVAIQAVLSLYAQGLSSG
VVVDSGDGVTHIVPVYESVVLNHLVGRLDVAGRDATRYLISLLLRKGYAF
NRTADFETVREMKEKLCYVSYDLELDHKLSEETTVLMRNYTLPDGRVIKV
GSERYECPECLFQPHLVGSEQPGLSEFIFDTIQAADVDIRKYLYRAIVLS
GGSSMYAGLPSRLEKEIKQLWFERVLHGDPARLPNFKVKIEDAPRRRHAV
FIGGAVLADIMAQNDHMWVSKAEWEEYGVRALDKLGP
3D structure
PDB8uxx High resolution cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by the Arp2/3 complex
ChainB
Resolution3.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 ATP B G11 T12 G13 F14 K16 G156 D157 G158 V159 R210 K213 E214 G302 M305 Y306 R347 G11 T12 G13 F14 K16 G156 D157 G158 V159 R210 K213 E214 G302 M305 Y306 R347
Gene Ontology
Molecular Function
GO:0003779 actin binding
GO:0005524 ATP binding
GO:0051015 actin filament binding
Biological Process
GO:0000147 actin cortical patch assembly
GO:0006897 endocytosis
GO:0034314 Arp2/3 complex-mediated actin nucleation
GO:0090135 actin filament branching
Cellular Component
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005885 Arp2/3 protein complex
GO:0005938 cell cortex
GO:0030479 actin cortical patch
GO:0031097 medial cortex
GO:0051285 cell cortex of cell tip

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8uxx, PDBe:8uxx, PDBj:8uxx
PDBsum8uxx
PubMed38448439
UniProtQ9UUJ1|ARP2_SCHPO Actin-related protein 2 (Gene Name=arp2)

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