Structure of PDB 4b1v Chain B

Receptor sequence

>4b1vB (length=359) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]

TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPGQKDSYVGDEAQSILT
LKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANR
EKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY
EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKL
CYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSF
IGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKE
ITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAG
PSIVHRKCF

3D structure

PDB

4b1v Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity.

Chain

Resolution

1.75 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Enzyme Commision number

3.6.4.-

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	peptide	B	Y143 T148 E167 G168 Y169 P172 H173 S350 T351 H371 R372 F375	Y127 T132 E151 G152 Y153 P156 H157 S334 T335 H355 R356 F359
BS02	ATP	B	G13 S14 G15 K18 G156 D157 G158 V159 G182 R210 K213 E214 G302 M305 Y306	G9 S10 G11 K14 G140 D141 G142 V143 G166 R194 K197 E198 G286 M289 Y290
BS03	LAB	B	G15 L16 P32 Q59 Y69 D157 T186 R206 E207 R210	G11 L12 P28 Q46 Y53 D141 T170 R190 E191 R194	BindingDB: IC50=8470nM

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003785	actin monomer binding
GO:0005509	calcium ion binding
GO:0005515	protein binding
GO:0005523	tropomyosin binding
GO:0005524	ATP binding
GO:0016787	hydrolase activity
GO:0019904	protein domain specific binding
GO:0031013	troponin I binding
GO:0031432	titin binding
GO:0032036	myosin heavy chain binding
GO:0042802	identical protein binding
GO:0048306	calcium-dependent protein binding
GO:0140660	cytoskeletal motor activator activity

	Biological Process
GO:0010628	positive regulation of gene expression
GO:0030041	actin filament polymerization
GO:0030240	skeletal muscle thin filament assembly
GO:0048741	skeletal muscle fiber development
GO:0051017	actin filament bundle assembly
GO:0090131	mesenchyme migration

	Cellular Component
GO:0001725	stress fiber
GO:0005737	cytoplasm
GO:0005856	cytoskeleton
GO:0005865	striated muscle thin filament
GO:0005884	actin filament
GO:0030027	lamellipodium
GO:0030175	filopodium
GO:0031941	filamentous actin
GO:0032432	actin filament bundle
GO:0044297	cell body
GO:0098723	skeletal muscle myofibril

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:4b1v, PDBe:4b1v, PDBj:4b1v
PDBsum	4b1v
PubMed	23041370
UniProt	P68135\|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

[Back to BioLiP]