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1R9Y

Bacterial cytosine deaminase D314A mutant.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004131molecular_functioncytosine deaminase activity
A0005829cellular_componentcytosol
A0006209biological_processcytosine catabolic process
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0019858biological_processcytosine metabolic process
A0035888molecular_functionisoguanine deaminase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0102480molecular_function5-fluorocytosine deaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 501
ChainResidue
AHIS61
AHIS63
AHIS214
AASP313
AMG502
AHOH604

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHOH603
AHOH604
AHOH605
AHOH606
AFE501
AHOH601
AHOH602

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AALA128
ALYS134
AGLU171
AARG174
ALEU175
AHOH798
AHOH984
AHOH984
AHOH1026

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715
ChainResidueDetails
AGLU217

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14
ChainResidueDetails
AHIS61
AHIS63
AHIS214
AASP313

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715
ChainResidueDetails
AGLN156

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144
ChainResidueDetails
ATRP319

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715
ChainResidueDetails
AHIS246

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 710
ChainResidueDetails
AHIS61metal ligand
AHIS63metal ligand
AGLN156electrostatic stabiliser
AHIS214metal ligand
AGLU217proton acceptor, proton donor
AASP313metal ligand

218853

PDB entries from 2024-04-24

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