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6NIB

Crystal Structure of Medicago truncatula Agmatine Iminohydrolase (Deiminase)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004668molecular_functionprotein-arginine deiminase activity
A0006596biological_processpolyamine biosynthetic process
A0009446biological_processputrescine biosynthetic process
A0016787molecular_functionhydrolase activity
A0033388biological_processputrescine biosynthetic process from arginine
A0047632molecular_functionagmatine deiminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 401
ChainResidue
AARG81
AARG81
AVAL149
AVAL149
AGLU150
AGLU150
AHOH855

site_idAC2
Number of Residues2
Detailsbinding site for residue GOL A 402
ChainResidue
AHOH745
AHOH875

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
ATRP19
AVAL232
AHOH507
AHOH780

site_idAC4
Number of Residues7
Detailsbinding site for residue NA A 404
ChainResidue
ATRP125
AASP219
AASP220
AASN222
AHOH854
AHOH886
AHOH979

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 405
ChainResidue
AARG73
AASN74
ALEU76
AHOH636
AHOH913
AHOH926

site_idAC6
Number of Residues12
Detailsbinding site for residue PEG A 406
ChainResidue
ATRP91
AASP94
AASP220
ATHR221
AHIS224
AGLY361
ACYS366
AHOH501
AHOH519
AHOH542
AHOH557
AHOH862

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Amidino-cysteine intermediate => ECO:0000250|UniProtKB:Q837U5
ChainResidueDetails
ACYS366

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30984210, ECO:0007744|PDB:6NIC
ChainResidueDetails
AASP220
AASP226

224004

PDB entries from 2024-08-21

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