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9C3F

Cryo-EM structure of E. coli AmpG

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005886cellular_componentplasma membrane
A0009055molecular_functionelectron transfer activity
A0009254biological_processpeptidoglycan turnover
A0015293molecular_functionsymporter activity
A0015647molecular_functionpeptidoglycan transmembrane transporter activity
A0015835biological_processpeptidoglycan transport
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022857molecular_functiontransmembrane transporter activity
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0071555biological_processcell wall organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:15728916
ChainResidueDetails
AMET1-GLN11

site_idSWS_FT_FI2
Number of Residues201
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:15728916
ChainResidueDetails
APRO12-SER32
APHE458-LEU485
ATHR48-PHE61
AGLY82-THR105
ALEU107-GLN124
AASN222-PHE240
ALYS265-GLN284
ALEU288-ASN303
ALEU328-ASN346
APRO422-LEU453

site_idSWS_FT_FI3
Number of Residues64
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:15728916
ChainResidueDetails
AGLY33-LYS47
AGLN106
AALA241-ASN264
AALA304-ASN327
ATHR454-SER457

site_idSWS_FT_FI4
Number of Residues191
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15728916
ChainResidueDetails
ALYS62-ARG81
AASP125-ARG221
AARG285-SER287
ALYS347-TYR421

site_idSWS_FT_FI5
Number of Residues5
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15728916, ECO:0000269|PubMed:15919996
ChainResidueDetails
AARG486-THR491

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP498
AILE593

237735

PDB entries from 2025-06-18

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