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5O5Q

X-ray crystal structure of RapZ from Escherichia coli (P3221 space group)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0050779biological_processRNA destabilization
A0051289biological_processprotein homotetramerization
A0060090molecular_functionmolecular adaptor activity
A0097367molecular_functioncarbohydrate derivative binding
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0050779biological_processRNA destabilization
B0051289biological_processprotein homotetramerization
B0060090molecular_functionmolecular adaptor activity
B0097367molecular_functioncarbohydrate derivative binding
C0000166molecular_functionnucleotide binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005525molecular_functionGTP binding
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0050779biological_processRNA destabilization
C0051289biological_processprotein homotetramerization
C0060090molecular_functionmolecular adaptor activity
C0097367molecular_functioncarbohydrate derivative binding
D0000166molecular_functionnucleotide binding
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0050779biological_processRNA destabilization
D0051289biological_processprotein homotetramerization
D0060090molecular_functionmolecular adaptor activity
D0097367molecular_functioncarbohydrate derivative binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG9
AGLY11
ASER12
AGLY13
ALYS14
ASER15

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 302
ChainResidue
AGLY249
AHIS252
AARG253
ASO4304
AASN188
ACYS247
ATHR248

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG184
AASN188
AARG253
BARG151

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 304
ChainResidue
AHIS190
AARG196
AHIS252
ASO4302

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 B 301
ChainResidue
BARG9
BSER10
BGLY11
BSER12
BGLY13
BLYS14
BSER15

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 B 302
ChainResidue
BARG101
BLEU102
BHIS103
BASN109
CTYR220
CARG223

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 B 303
ChainResidue
BASN188
BHIS190
BCYS247
BTHR248
BGLY249
BHIS252
BARG253

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 D 301
ChainResidue
ATYR220
AARG223
DARG101
DLEU102
DHIS103
DASN109

site_idAC9
Number of Residues7
Detailsbinding site for residue SO4 D 302
ChainResidue
DARG9
DSER10
DGLY11
DSER12
DGLY13
DLYS14
DSER15

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 D 303
ChainResidue
DGLY11
DARG95
DVAL141
DSO4306

site_idAD2
Number of Residues2
Detailsbinding site for residue SO4 D 304
ChainResidue
DSER97
DARG100

site_idAD3
Number of Residues1
Detailsbinding site for residue SO4 D 306
ChainResidue
DSO4303

site_idAD4
Number of Residues5
Detailsbinding site for residue SO4 C 301
ChainResidue
CASN188
CHIS190
CTHR248
CGLY249
CARG253

site_idAD5
Number of Residues8
Detailsbinding site for Di-peptide SO4 C 302 and LYS C 14
ChainResidue
CARG9
CGLY11
CSER12
CGLY13
CSER15
CVAL16
CALA17
CLEU18

site_idAD6
Number of Residues11
Detailsbinding site for Di-peptide SO4 D 305 and ARG D 253
ChainResidue
DARG184
DPRO187
DASN188
DCYS247
DTHR248
DGLY249
DHIS252
DSER254
DVAL255
DTYR256
DILE257

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00636
ChainResidueDetails
AGLY8
AASP56
BGLY8
BASP56
DGLY8
DASP56
CGLY8
CASP56

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS251
BLYS251
DLYS251
CLYS251

218853

数据于2024-04-24公开中

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