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3A6V

Crystal structure of the MutT protein in MN(II) bound holo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0006203biological_processdGTP catabolic process
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006974biological_processDNA damage response
A0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
A0044715molecular_function8-oxo-dGDP phosphatase activity
A0044716molecular_function8-oxo-GDP phosphatase activity
A0046067biological_processdGDP catabolic process
A0046872molecular_functionmetal ion binding
A0047693molecular_functionATP diphosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0006203biological_processdGTP catabolic process
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006974biological_processDNA damage response
B0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0030145molecular_functionmanganese ion binding
B0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
B0044715molecular_function8-oxo-dGDP phosphatase activity
B0044716molecular_function8-oxo-GDP phosphatase activity
B0046067biological_processdGDP catabolic process
B0046872molecular_functionmetal ion binding
B0047693molecular_functionATP diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 1003
ChainResidue
AGLU53
AGLU57
AHOH132
AHOH133
BASP77
BHOH132

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 1004
ChainResidue
BHOH132
BHOH138
BTLA2001
AGLU53
AHOH131
AHOH134

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1005
ChainResidue
AGLY37
AGLU57
AHOH153
BASP77
BHOH186

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TLA A 2002
ChainResidue
ALYS39
AARG78
AHOH149
BLYS39
BARG78

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA A 2003
ChainResidue
ALYS2
AARG78
AHOH138
BGLU41
BHOH134
BHOH135
BHOH150
BMN1002

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 1001
ChainResidue
AASP77
AHOH136
BGLU53
BGLU57
BHOH137
BHOH181

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 1002
ChainResidue
AHOH136
AHOH138
ATLA2003
BGLU53
BHOH134
BHOH135

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 1006
ChainResidue
AASP77
AHOH163
BGLY37
BGLU57
BHOH140

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TLA B 2001
ChainResidue
AGLU41
AHOH131
AHOH134
AHOH158
AHOH191
AMN1004
BLYS2
BARG78
BHOH132
BHOH138
BHOH142

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GkiemgEtpeqAVvRELqEEvG
ChainResidueDetails
AGLY38-GLY59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:19864691
ChainResidueDetails
AARG23
AHIS28
AGLU34
BARG23
BHIS28
BGLU34

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19864691
ChainResidueDetails
AGLY37
AGLU57
BGLY37
BGLU57

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12939141, ECO:0000305|PubMed:19864691
ChainResidueDetails
AASN119
BASN119

218853

PDB entries from 2024-04-24

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