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9B70

Cryo-EM structure of MraY in complex with analogue 2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0042802molecular_functionidentical protein binding
A0044038biological_processcell wall macromolecule biosynthetic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016740molecular_functiontransferase activity
B0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
B0042802molecular_functionidentical protein binding
B0044038biological_processcell wall macromolecule biosynthetic process
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS01347
Number of Residues13
DetailsMRAY_1 MraY family signature 1. KkyTPTMGGIvIL
ChainResidueDetails
BLYS70-LEU82

site_idPS01348
Number of Residues12
DetailsMRAY_2 MraY family signature 2. NavNlTDGLDGL
ChainResidueDetails
BASN187-LEU198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues136
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:23990562
ChainResidueDetails
BMET1-ARG25
AHIS219-TYR233
ALEU281-SER284
ALEU356-ARG359
BMET93-LYS98
BASP153-VAL172
BHIS219-TYR233
BLEU281-SER284
BLEU356-ARG359
AMET1-ARG25
AMET93-LYS98
AASP153-VAL172

site_idSWS_FT_FI2
Number of Residues44
DetailsTRANSMEM: Helical; Name=Helix 1 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BSER26-LEU48
ASER26-LEU48

site_idSWS_FT_FI3
Number of Residues130
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23990562
ChainResidueDetails
BARG49-PRO74
ATRP311-LEU332
BLYS121-ILE130
BLEU195-GLY197
BSER256-GLY264
BTRP311-LEU332
AARG49-PRO74
ALYS121-ILE130
ALEU195-GLY197
ASER256-GLY264

site_idSWS_FT_FI4
Number of Residues34
DetailsTRANSMEM: Helical; Name=Helix 2 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BTHR75-LEU92
ATHR75-LEU92

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=Helix 3 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BTYR99-VAL120
ATYR99-VAL120

site_idSWS_FT_FI6
Number of Residues42
DetailsTRANSMEM: Helical; Name=Helix 4 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BLYS131-ALA152
ALYS131-ALA152

site_idSWS_FT_FI7
Number of Residues42
DetailsTRANSMEM: Helical; Name=Helix 5 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BLEU173-GLY194
ALEU173-GLY194

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=Helix 6 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BLEU198-GLY218
ALEU198-GLY218

site_idSWS_FT_FI9
Number of Residues42
DetailsTRANSMEM: Helical; Name=Helix 7 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BALA234-ASN255
AALA234-ASN255

site_idSWS_FT_FI10
Number of Residues30
DetailsTRANSMEM: Helical; Name=Helix 8 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BASP265-LEU280
AASP265-LEU280

site_idSWS_FT_FI11
Number of Residues50
DetailsTRANSMEM: Helical; Name=Helix 9 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BGLU285-ARG310
AGLU285-ARG310

site_idSWS_FT_FI12
Number of Residues44
DetailsTRANSMEM: Helical; Name=Helix 10 => ECO:0000269|PubMed:23990562
ChainResidueDetails
BPRO333-MET355
APRO333-MET355

site_idSWS_FT_FI13
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR
ChainResidueDetails
BLYS70
ALYS70
ATHR75
AASN190
AASP193
AASP196
AGLY264
ASER268
AGLN305
AALA321
BTHR75
BASN190
BASP193
BASP196
BGLY264
BSER268
BGLN305
BALA321

226262

PDB entries from 2024-10-16

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