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6ZHL

Crystal Structure of Staphylococcus aureus RsgA bound to ppGpp.

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
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue G4P A 301
ChainResidue
AARG28
ASER166
AGLY167
AVAL168
AGLY169
ALYS170
ASER171
ATHR172
AHOH465
AHOH466
AARG32
ALYS113
AASP115
ALYS116
AGLY143
AASN144
AARG148
AGLN165

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
ACYS245
ACYS250
AHIS252
ACYS258

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 303
ChainResidue
AARG68
ATYR103
APHE218
AALA220
AASP222
AHOH451

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
ASER89
ATHR90
AGLN91
AEDO305

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 305
ChainResidue
AHIS276
AEDO304
AHOH447

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 306
ChainResidue
AASN134
AGLY267
AALA270

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 307
ChainResidue
AARG108
AGLU138
AALA154
ATRP155
APRO156

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 308
ChainResidue
AASN134
AILE135
AGLU237
AARG240
AASN268
AHOH409
AHOH429

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 309
ChainResidue
AGLU133
ATHR139
AGLU140
AHOH416
AHOH422

site_idAD1
Number of Residues3
Detailsbinding site for residue PGE A 310
ChainResidue
ALYS35
APHE36
AVAL59

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 Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01820
ChainResidueDetails
ATHR112
AGLY164
ACYS245
ACYS250
AHIS252
ACYS258

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PDB entries from 2025-06-11

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