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2CI5

Crystal structure of Dimethylarginine Dimethylaminohydrolase I in complex with L-homocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000052biological_processcitrulline metabolic process
A0006525biological_processarginine metabolic process
A0006809biological_processnitric oxide biosynthetic process
A0008270molecular_functionzinc ion binding
A0009891biological_processpositive regulation of biosynthetic process
A0016403molecular_functiondimethylargininase activity
A0016597molecular_functionamino acid binding
A0016787molecular_functionhydrolase activity
A0017014biological_processprotein nitrosylation
A0030235molecular_functionnitric-oxide synthase regulator activity
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0046872molecular_functionmetal ion binding
B0000052biological_processcitrulline metabolic process
B0006525biological_processarginine metabolic process
B0006809biological_processnitric oxide biosynthetic process
B0008270molecular_functionzinc ion binding
B0009891biological_processpositive regulation of biosynthetic process
B0016403molecular_functiondimethylargininase activity
B0016597molecular_functionamino acid binding
B0016787molecular_functionhydrolase activity
B0017014biological_processprotein nitrosylation
B0030235molecular_functionnitric-oxide synthase regulator activity
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HCS A1281
ChainResidue
ALEU29
AHOH2316
AASP72
APHE75
AASP78
AARG97
AARG144
AVAL267
AASP268
ACYS273

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HCS B1281
ChainResidue
BLEU29
BASP72
BPHE75
BASP78
BARG97
BARG144
BVAL267
BASP268
BCYS273
BHOH2308

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT B1282
ChainResidue
ALYS195
AILE199
AHOH2217
BARG41
BARG44
BGLN45
BLEU48
BSER260
BHOH2279
BHOH2318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"12441345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jdw
ChainResidueDetails
ACYS273
AHIS172
AASP126

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jdw
ChainResidueDetails
BCYS273
BHIS172
BASP126

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PDB entries from 2025-12-17

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