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Calcium free form of human peptidylarginine deiminase type4 (PAD4) External Resource: Annotation Chains Domain Info Class Fold Superfamily Family Domain Species Provenance Source (Version) A d1wd8a1 All beta proteins Common fold of diphtheria toxin/transcription factors/cytochrome f Peptidylarginine deiminase Pad4, middle domain Peptidylarginine deiminase Pad4, middle domain Peptidylarginine deiminase Pad4, middle domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08) A d1wd8a2 All beta proteins Cupredoxin-like Cupredoxins Peptidylarginine deiminase Pad4, N-terminal domain Peptidylarginine deiminase Pad4, N-terminal domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08) A d1wd8a3 Alpha and beta proteins (a+b) Pentein, beta/alpha-propeller Pentein Peptidylarginine deiminase Pad4, catalytic C-terminal domain Peptidylarginine deiminase Pad4, catalytic C-terminal domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2B Superfamily Pentein 8039686 3000640 SCOP2B (2022-06-29) A SCOP2B Superfamily Cupredoxins 8039685 3000886 SCOP2B (2022-06-29) A SCOP2B Superfamily Peptidylarginine deiminase Pad4 middle domain 8039684 3000247 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A PF08527 e1wd8A3 A: beta sandwiches X: Immunoglobulin-like beta-sandwich H: Immunoglobulin-related T: Common fold of diphtheria toxin/transcription factors/cytochrome f F: PF08527 ECOD (1.6) A PF08526 e1wd8A4 A: beta sandwiches X: Cupredoxin-like H: Cupredoxin-related (From Topology) T: Cupredoxin-related F: PF08526 ECOD (1.6) A PF03068 e1wd8A1 A: a+b duplicates or obligate multimers X: Pentein (From Topology) H: Pentein (From Topology) T: Pentein F: PF03068 ECOD (1.6)
Chains Polymer Molecular Function Biological Process Cellular Component Protein-arginine deiminase type IV
Chains Drug Target   Associated Disease Pharos :  Q9UM07
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage Chains Enzyme Name Description Catalytic Residues protein-arginine deiminase
M-CSA #594 In the presence of calcium ions, Protein-arginine deiminase (PAD) enzymes catalyse the post-translational modification reaction responsible for the formation of citrulline residues from protein-bound arginine residues. The gene for this enzyme is a susceptibility locus for rheumatoid arthritis.
 View MoreDefined by 4 residues: ASP:A-357 [auth A-350] HIS:A-478 [auth A-471] ASP:A-480 [auth A-473] CYS:A-652 [auth A-645]
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M-CSA Motif Definition