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3LHL

Crystal structure of a putative agmatinase from Clostridium difficile

Functional Information from GO Data
ChainGOidnamespacecontents
A0008783molecular_functionagmatinase activity
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0033389biological_processputrescine biosynthetic process from arginine, using agmatinase
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AHIS111
AASP134
AASP138
AASP215
AMN302
AMN303

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AASP217
AMN301
AMN303
AASP134
AHIS136
AASP215

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 303
ChainResidue
AASP138
AHIS150
AASP215
AGLU261
AMN301
AMN302

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 304
ChainResidue
AASN236
AASN236
AASN236

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 305
ChainResidue
ATHR34
ASER35
AASN36
AARG37
ATYR143
AHIS150
AHOH323

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 306
ChainResidue
AARG99
ATYR143
AASN144
AASN145
AHOH364
AHOH419
AHOH431

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 307
ChainResidue
AHOH6
APHE26
AGLY27
ASER44
AARG48
AASP72

Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. TIDLDvldAsvfPGtgtpepgG
ChainResidueDetails
ATHR213-GLY234

221051

PDB entries from 2024-06-12

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