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3RHY

Crystal structure of the dimethylarginine dimethylaminohydrolase adduct with 4-chloro-2-hydroxymethylpyridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000052biological_processcitrulline metabolic process
A0006525biological_processarginine metabolic process
A0016403molecular_functiondimethylargininase activity
A0016597molecular_functionamino acid binding
A0016787molecular_functionhydrolase activity
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0046872molecular_functionmetal ion binding
B0000052biological_processcitrulline metabolic process
B0006525biological_processarginine metabolic process
B0016403molecular_functiondimethylargininase activity
B0016597molecular_functionamino acid binding
B0016787molecular_functionhydrolase activity
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HM3 A 255
ChainResidue
APHE63
AASP66
AHIS162
AASP244
ACYS249

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HM3 B 255
ChainResidue
BCYS249
BPHE63
BHIS162
BASP244
BGLY245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:11473257, ECO:0000305|PubMed:16634643, ECO:0000305|PubMed:18482699
ChainResidueDetails
AHIS162
BHIS162

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11473257, ECO:0000305|PubMed:16634643, ECO:0000305|PubMed:18482699
ChainResidueDetails
ACYS249
BCYS249

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:11473257
ChainResidueDetails
ALEU18
BARG85
BARG132
BILE243
AASP60
AGLU65
AARG85
AARG132
AILE243
BLEU18
BASP60
BGLU65

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:16634643
ChainResidueDetails
AHIS162
ACYS249
BHIS162
BCYS249

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PDB entries from 2024-07-31

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