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1P6O

The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004131molecular_functioncytosine deaminase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0008655biological_processpyrimidine-containing compound salvage
A0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A0016787molecular_functionhydrolase activity
A0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A0019239molecular_functiondeaminase activity
A0019858biological_processcytosine metabolic process
A0034654biological_processnucleobase-containing compound biosynthetic process
A0044206biological_processUMP salvage
A0046087biological_processcytidine metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004131molecular_functioncytosine deaminase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0008655biological_processpyrimidine-containing compound salvage
B0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B0016787molecular_functionhydrolase activity
B0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
B0019239molecular_functiondeaminase activity
B0019858biological_processcytosine metabolic process
B0034654biological_processnucleobase-containing compound biosynthetic process
B0044206biological_processUMP salvage
B0046087biological_processcytidine metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 400
ChainResidue
BHIS262
BCYS291
BCYS294
BHPY410

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS62
ACYS91
ACYS94
AHPY411

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BGLU328
BGLN350
BHOH1016
BHOH1060
BHOH1237
AGLU75

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
AGLN150
AHOH1231
AHOH1311
BGLU275
BHOH1312
BHOH1392

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HPY B 410
ChainResidue
BILE233
BASN251
BHIS262
BGLY263
BGLU264
BPRO290
BCYS291
BCYS294
BASP355
BZN400

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HPY A 411
ChainResidue
AILE33
AASN51
AHIS62
AGLY63
AGLU64
APRO90
ACYS91
ACYS94
AASP155
AZN401

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 420
ChainResidue
AASP42
AHOH1214
AHOH1222
AHOH1228
BARG273

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 421
ChainResidue
BGLY302
BGLY326
BHIS327
BPHE353
BHOH1093
BHOH1188

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 422
ChainResidue
ALYS77
BASN240
BASP281
BPRO304
BPHE353
BHOH1105
BHOH1162

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues37
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HGEisTLencgrlegkvykdttlyttls............PCdm......CtgaI
ChainResidueDetails
AHIS62-ILE98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ
ChainResidueDetails
AGLU64
BGLU264

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
ChainResidueDetails
AASN51
AASP155
BASN251
BASP355

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
ChainResidueDetails
AHIS62
ACYS91
ACYS94
BHIS262
BCYS291
BCYS294

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1uaq
ChainResidueDetails
AGLU64
ACYS91
ASER89

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1uaq
ChainResidueDetails
BGLU264
BCYS291
BSER289

site_idMCSA1
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
AHIS62metal ligand
AGLU64proton acceptor, proton donor
ASER89electrostatic stabiliser
ACYS91metal ligand
ACYS94metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 636
ChainResidueDetails
BHIS262metal ligand
BGLU264proton acceptor, proton donor
BSER289electrostatic stabiliser
BCYS291metal ligand
BCYS294metal ligand

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PDB entries from 2024-11-06

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