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6ZJO

Crystal Structure of Staphylococcus aureus RsgA.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0019843molecular_functionrRNA binding
A0042254biological_processribosome biogenesis
A0042274biological_processribosomal small subunit biogenesis
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0019843molecular_functionrRNA binding
B0042254biological_processribosome biogenesis
B0042274biological_processribosomal small subunit biogenesis
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS245
ACYS250
AHIS252
ACYS258

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 302
ChainResidue
AMET1
AHOH402

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 303
ChainResidue
AGLN58
BLYS130

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO A 304
ChainResidue
ASER82
APRO86
AASN87
ASER89
ALEU92
AGLN165
AVAL168
AMET81

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 305
ChainResidue
AARG148
ATHR172
AHIS176

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 306
ChainResidue
AVAL59
AGLU61

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 307
ChainResidue
AASN286
AEDO308
AHOH404
AHOH405

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO A 308
ChainResidue
AEDO307
AHOH404

site_idAC9
Number of Residues7
Detailsbinding site for residue PO4 A 309
ChainResidue
ASER166
AGLY167
AVAL168
AGLY169
ALYS170
ASER171
AHOH457

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS245
BCYS250
BHIS252
BCYS258

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
AGLY158
AHOH429
BPRO118
BGLU120

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BASN126
BLEU129
BLYS130
BPHE141
BHOH475

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO B 304
ChainResidue
BPHE88
BSER89
BTHR90
BGLN91

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 306
ChainResidue
BASP146
BASP147
BARG148
BHIS176

site_idAD6
Number of Residues3
Detailsbinding site for residue EDO B 307
ChainResidue
BPRO69
BHIS201
BHOH478

site_idAD7
Number of Residues1
Detailsbinding site for residue EDO B 308
ChainResidue
BSER219

site_idAD8
Number of Residues6
Detailsbinding site for residue EDO B 309
ChainResidue
AGLU120
BASN19
BTYR211
BLYS254
BPO4312
BHOH453

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO B 310
ChainResidue
BGLU203
BPHE205
BALA213
BASP214

site_idAE1
Number of Residues5
Detailsbinding site for residue PO4 B 311
ChainResidue
BGLY167
BVAL168
BGLY169
BLYS170
BSER171

site_idAE2
Number of Residues8
Detailsbinding site for residue PO4 B 312
ChainResidue
APRO118
AGLU120
ALYS121
BALA157
BGLY158
BASN209
BEDO309
BHOH403

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. IVLsGQSGVGKstF
ChainResidueDetails
AILE160-PHE173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01820","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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