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5CKR

Crystal Structure of MraY in complex with Muraymycin D2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0007049biological_processcell cycle
A0008360biological_processregulation of cell shape
A0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
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
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue 57M A 401
ChainResidue
ALYS70
AMET263
AGLY264
AASP265
ASER268
AVAL302
AGLN305
AARG320
AALA321
APRO322
AHIS325
ATHR75
AHOH503
AASN190
AASP193
AGLY194
ALEU195
AASP196
AASN255
APHE262

Functional Information from PROSITE/UniProt
site_idPS01347
Number of Residues13
DetailsMRAY_1 MraY family signature 1. KkyTPTMGGIvIL
ChainResidueDetails
ALYS70-LEU82

site_idPS01348
Number of Residues12
DetailsMRAY_2 MraY family signature 2. NavNlTDGLDGL
ChainResidueDetails
AASN187-LEU198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues68
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:23990562
ChainResidueDetails
AMET1-ARG25
AMET93-LYS98
AASP153-VAL172
AHIS219-TYR233
ALEU281-SER284
ALEU356-ARG359

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=Helix 1 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ASER26-LEU48

site_idSWS_FT_FI3
Number of Residues65
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23990562
ChainResidueDetails
AARG49-PRO74
ALYS121-ILE130
ALEU195-GLY197
ASER256-GLY264
ATRP311-LEU332

site_idSWS_FT_FI4
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix 2 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ATHR75-LEU92

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix 3 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ATYR99-VAL120

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix 4 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ALYS131-ALA152

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix 5 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ALEU173-GLY194

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=Helix 6 => ECO:0000269|PubMed:23990562
ChainResidueDetails
ALEU198-GLY218

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix 7 => ECO:0000269|PubMed:23990562
ChainResidueDetails
AALA234-ASN255

site_idSWS_FT_FI10
Number of Residues15
DetailsTRANSMEM: Helical; Name=Helix 8 => ECO:0000269|PubMed:23990562
ChainResidueDetails
AASP265-LEU280

site_idSWS_FT_FI11
Number of Residues25
DetailsTRANSMEM: Helical; Name=Helix 9 => ECO:0000269|PubMed:23990562
ChainResidueDetails
AGLU285-ARG310

site_idSWS_FT_FI12
Number of Residues22
DetailsTRANSMEM: Helical; Name=Helix 10 => ECO:0000269|PubMed:23990562
ChainResidueDetails
APRO333-MET355

site_idSWS_FT_FI13
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:27088606, ECO:0007744|PDB:5CKR
ChainResidueDetails
ALYS70
ATHR75
AASN190
AASP193
AASP196
AGLY264
ASER268
AGLN305
AALA321

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PDB entries from 2024-03-27

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