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2CZ8

Crystal Structure of tt0972 protein from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
B0000166molecular_functionnucleotide binding
C0000166molecular_functionnucleotide binding
D0000166molecular_functionnucleotide binding
E0000166molecular_functionnucleotide binding
F0000166molecular_functionnucleotide binding
G0000166molecular_functionnucleotide binding
H0000166molecular_functionnucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 2101
ChainResidue
ALYS6
AVAL8
AHOH2178
BLYS6
BVAL8
CLYS6
CVAL8

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 D 2102
ChainResidue
DLYS6
DLYS6
DLYS6

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 E 2103
ChainResidue
ELYS6
EVAL8
EHOH2106
EHOH2125
EHOH2184
FLYS6
FVAL8
GLYS6
GVAL8

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 H 2104
ChainResidue
HLYS6
HLYS6
HLYS6

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 2105
ChainResidue
BTHR13
BSER14
BGLU55
BHOH2127
BHOH2140
BHOH2170
CGLY2
CLYS3

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D 2106
ChainResidue
DGLY2
DLYS3
DTHR13
DSER14
DGLU55
DHOH2138
DHOH2160
DHOH2179

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 F 2107
ChainResidue
FTHR13
FSER14
FGLU55
FHOH2134
FHOH2155
GGLY2
GLYS3

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 H 2108
ChainResidue
HGLY2
HLYS3
HTHR13
HSER14
HGLU55
HHOH2137
HHOH2165
HHOH2171
HHOH2177

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 G 2109
ChainResidue
EGLY2
ELYS3
GTHR13
GSER14
GGLU15
GGLU55
GHOH2135
GHOH2166

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 1150
ChainResidue
AGLU19
AGLU19
AGLU19

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K C 1151
ChainResidue
BGLU19
CGLU19
DGLU19

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K E 1152
ChainResidue
EGLU19
EGLU19
EGLU19

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K G 1153
ChainResidue
FGLU19
GGLU19
HGLU19

site_idBC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FAD A 1201
ChainResidue
ALYS3
ATYR5
ALEU33
AARG34
AHIS35
ALEU36
AASP37
ATRP38
AARG45
ATHR47
AGLN57
AARG65
AHOH2110
AHOH2159
AHOH2160
AHOH2161
AHOH2163
AHOH2169
BFAD1202
CVAL11
CGLN57
CVAL59

site_idBC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FAD B 1202
ChainResidue
BLYS3
BTYR5
BHIS35
BASP37
BTRP38
BARG65
BHOH2145
BHOH2161
BHOH2167
CARG45
CTHR47
CGLN57
CHOH1257
AVAL11
AGLN57
AFAD1201

site_idBC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FAD C 1203
ChainResidue
BGLN57
BHOH2150
BHOH2187
CLYS3
CTYR5
CGLU16
CHIS35
CASP37
CTRP38
CARG65
CHOH1224
CHOH1269
CHOH1270
CHOH1279
CHOH1281
DARG45
DTHR47
DGLN57
DFAD1204
DHOH2132

site_idBC8
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FAD D 1204
ChainResidue
BARG45
BTHR47
BILE48
BGLU50
BGLN57
CFAD1203
DLYS3
DTYR5
DVAL11
DARG34
DHIS35
DLEU36
DASP37
DTRP38
DGLN57
DARG65
DHOH2115
DHOH2174
EGLU50
EALA51

site_idBC9
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FAD E 1205
ChainResidue
ELYS3
ETYR5
EARG30
EARG34
EHIS35
EASP37
ETRP38
EARG45
ETHR47
EGLN57
EARG65
EHOH2156
EHOH2164
EHOH2165
EHOH2166
EHOH2167
EHOH2181
FFAD1206
GVAL11
GGLN57
GVAL59
GHOH2120

site_idCC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FAD F 1206
ChainResidue
EVAL11
EGLN57
EFAD1205
FLYS3
FTYR5
FARG30
FLEU33
FARG34
FHIS35
FLEU36
FASP37
FTRP38
FARG65
FHOH2153
FHOH2159
FHOH2160
FHOH2167
GARG45
GTHR47
GGLN57

site_idCC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FAD G 1207
ChainResidue
FGLN57
FHOH2182
GLYS3
GTYR5
GGLU16
GHIS35
GASP37
GTRP38
GARG65
GHOH2122
GHOH2147
GHOH2164
GHOH2165
GHOH2176
GHOH2180
HARG45
HTHR47
HGLN57
HFAD1208

site_idCC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FAD H 1208
ChainResidue
FARG45
FTHR47
FGLN57
GFAD1207
HLYS3
HTYR5
HVAL11
HARG34
HHIS35
HLEU36
HASP37
HTRP38
HGLN57
HVAL59
HARG65
HHOH2118
HHOH2181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2008","submissionDatabase":"PDB data bank","title":"Ultrafast charge transfer dynamics in flavoprotein dodecin.","authors":["Gurzadyan G.G.","Meissner B.","Sander B.","Essen L.-O.","Michel-Beyerle M.E."]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2008","submissionDatabase":"PDB data bank","title":"Ultrafast charge transfer dynamics in flavoprotein dodecin.","authors":["Gurzadyan G.G.","Meissner B.","Sander B.","Essen L.-O.","Michel-Beyerle M.E."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"description":"in other chain"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"May be important for ligand binding specificity and FMN binding"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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