Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FCL

Complex of UNG2 and a fragment-based designed inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0004844molecular_functionuracil DNA N-glycosylase activity
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 3FL A 1
ChainResidue
AHOH20
ASER273
AHOH339
AHOH400
BGLU83
BPHE84
BPHE85
BLYS90
BHOH444
AGLY143
AGLN144
AASP145
ATYR147
ACYS157
APHE158
AASN204
ASER270

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 2
ChainResidue
AMET106
AVAL109
AARG113
AVAL125
BARG276

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN A 5
ChainResidue
ATYR147
APRO167
ASER169
AHOH397
AHOH427
BSCN8

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SCN A 6
ChainResidue
APRO168
AASN172
APRO271
AHOH336
BGLY98
BILE103
BHOH449

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 7
ChainResidue
ASER270
AHOH399
BSCN8
BLYS90
BPHE97

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 3FL B 2
ChainResidue
AGLU83
APHE84
AHOH367
BSCN4
BHOH47
BGLY143
BGLN144
BASP145
BTYR147
BCYS157
BPHE158
BSER169
BASN204
BHIS268
BSER270
BSER273
BHOH327
BHOH346
BHOH386
BHOH499
BHOH500

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN B 1
ChainResidue
BMET106
BVAL109
BARG113
BVAL125

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN B 3
ChainResidue
BPHE184
BILE299
BTRP301
BLYS302

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN B 4
ChainResidue
ALYS90
APHE97
B3FL2
BSER270
BPRO271

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN B 8
ChainResidue
ASCN5
ASCN7
APRO168
APRO271
BSER94

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS138-TYR147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03166
ChainResidueDetails
AASP145
BASP145

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS286
BLYS286

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP145
AHIS268

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
BASP145
BHIS268

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon