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1KQJ

Crystal Structure of a Mutant of MutY Catalytic Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019104molecular_functionDNA N-glycosylase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
APRO69
ALEU70
AHOH427
AHOH603

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
ACYS192
AHIS199
ACYS202
ACYS208

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
ATHR43
AARG58
AASP64
AGLY79
ALEU80
AGLY81
AHOH538
AGLN42

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ATYR31
ATHR61
AVAL62
ALYS103
APHE104
AHOH444
AHOH466

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AARG87
AASN88
ALYS91
AHOH467

Functional Information from PROSITE/UniProt
site_idPS01155
Number of Residues30
DetailsENDONUCLEASE_III_2 Endonuclease III family signature. GkFPetfeeVaa.LPGVGrstAgaiLslSLG
ChainResidueDetails
AGLY102-GLY131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P83847
ChainResidueDetails
AGLU37

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ACYS192
AHIS199
ACYS202
ACYS208

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P83847
ChainResidueDetails
AASP138

221051

PDB entries from 2024-06-12

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