Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9B96

Crystal structure of the human PAD2 protein bound to inhibitor

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000791	cellular_component	euchromatin
A	0004668	molecular_function	protein-arginine deiminase activity
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006338	biological_process	chromatin remodeling
A	0016787	molecular_function	hydrolase activity
A	0021762	biological_process	substantia nigra development
A	0030331	molecular_function	nuclear estrogen receptor binding
A	0030520	biological_process	estrogen receptor signaling pathway
A	0035578	cellular_component	azurophil granule lumen
A	0042803	molecular_function	protein homodimerization activity
A	0045815	biological_process	transcription initiation-coupled chromatin remodeling
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	0070100	biological_process	negative regulation of chemokine-mediated signaling pathway
A	0140794	molecular_function	histone arginine deiminase activity
A	0140795	molecular_function	histone H3R2 arginine deiminase activity
A	0140796	molecular_function	histone H3R8 arginine deiminase activity
A	0140797	molecular_function	histone H3R17 arginine deiminase activity
A	0140798	molecular_function	histone H3R26 arginine deiminase activity
A	0140809	molecular_function	histone H4R3 arginine deiminase activity
A	0140810	molecular_function	histone H1R54 arginine deiminase activity
A	0140811	molecular_function	histone H2AR3 arginine deiminase activity
A	1901624	biological_process	negative regulation of lymphocyte chemotaxis
A	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:25621824

Chain	Residue	Details
A	CYS647

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N20, ECO:0007744\|PDB:4N22, ECO:0007744\|PDB:4N24, ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2F, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2H, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2M, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASP123

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N20, ECO:0007744\|PDB:4N22, ECO:0007744\|PDB:4N24, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2D, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2F, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2H, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2K, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2M, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASP125

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N20, ECO:0007744\|PDB:4N22, ECO:0007744\|PDB:4N24, ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2D, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2F, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2H, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2K, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2M, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASP127
A	VAL129
A	GLU131

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASN154
A	ASP389

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASP156
A	ASP180

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	GLU158

site_id	SWS_FT_FI8
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2I, ECO:0007744\|PDB:4N2L

Chain	Residue	Details
A	ASP166
A	ASP169
A	LYS171

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:4N25, ECO:0007744\|PDB:4N26, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2A, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2G, ECO:0007744\|PDB:4N2L, ECO:0007744\|PDB:4N2N

Chain	Residue	Details
A	ASP177

site_id	SWS_FT_FI10
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2I

Chain	Residue	Details
A	GLU354

site_id	SWS_FT_FI11
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:25621824, ECO:0007744\|PDB:4N28, ECO:0007744\|PDB:4N2B, ECO:0007744\|PDB:4N2C, ECO:0007744\|PDB:4N2E, ECO:0007744\|PDB:4N2I

Chain	Residue	Details
A	PHE408
A	LEU411
A	GLU412

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)