8GOD

Co-crystal structure of Human Protein-arginine deiminase type-4 (PAD4) with small molecule inhibitor JBI-589

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004668	molecular_function	protein-arginine deiminase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006334	biological_process	nucleosome assembly
A	0006338	biological_process	chromatin remodeling
A	0016787	molecular_function	hydrolase activity
A	0019827	biological_process	stem cell population maintenance
A	0032991	cellular_component	protein-containing complex
A	0036211	biological_process	protein modification process
A	0042802	molecular_function	identical protein binding
A	0043687	biological_process	post-translational protein modification
A	0045087	biological_process	innate immune response
A	0046872	molecular_function	metal ion binding
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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15247907

Chain	Residue	Details
A	ASP350
A	HIS471
A	ASP473
A	CYS645

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site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269|PubMed:15247907, ECO:0000269|PubMed:16567635, ECO:0000269|PubMed:17002273

Chain	Residue	Details
A	ASN153
A	GLU351
A	GLU353
A	ASP369
A	SER370
A	ASN373
A	ASP388
A	PHE407
A	LEU410
A	GLU411
A	ASP155
A	ASP157
A	ASP165
A	ASP168
A	GLU170
A	ASP176
A	ASP179
A	GLN349

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21882827

Chain	Residue	Details
A	ARG374
A	ARG639

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site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Citrulline => ECO:0000269|PubMed:20201080

Chain	Residue	Details
A	ARG205
A	ARG212
A	ARG218
A	ARG372
A	ARG374
A	ARG383

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 594

Chain	Residue	Details
A	ASP350	electrostatic stabiliser
A	HIS471	proton acceptor, proton donor
A	ASP473	electrostatic stabiliser
A	CYS645	nucleofuge, nucleophile, proton acceptor, proton donor

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