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4IZ6

Structure of EntE and EntB, an NRPS adenylation-PCP fusion protein with pseudo translational symmetry

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0008668molecular_function2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
A0009239biological_processenterobactin biosynthetic process
A0016020cellular_componentmembrane
A0016746molecular_functionacyltransferase activity
A0016874molecular_functionligase activity
A0019290biological_processsiderophore biosynthetic process
A0047527molecular_function2,3-dihydroxybenzoate-serine ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0008668molecular_function2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
B0009239biological_processenterobactin biosynthetic process
B0016020cellular_componentmembrane
B0016746molecular_functionacyltransferase activity
B0016874molecular_functionligase activity
B0019290biological_processsiderophore biosynthetic process
B0047527molecular_function2,3-dihydroxybenzoate-serine ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 1HZ A 701
ChainResidue
AASN235
AMET334
AALA335
AVAL339
AGLN355
AASP415
ALYS432
ALYS441
AHOH898
BPNS702
ATYR236
ASER240
AGLY309
AALA310
AARG311
AVAL331
APHE332
AGLY333

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PNS A 702
ChainResidue
ASER575
AHOH829
AHOH830
AHOH845
AHOH848
AHOH857
AHOH879
BILE230
BPRO231
BHIS234
BTYR236
BVAL279
BGLY438
BGLY439
BGLU440
B1HZ701

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 1HZ B 701
ChainResidue
APNS702
BASN235
BTYR236
BSER240
BGLY309
BALA310
BARG311
BVAL331
BPHE332
BGLY333
BVAL339
BASP415
BVAL427
BLYS441
BHOH820
BHOH821

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PNS B 702
ChainResidue
APRO231
AHIS234
AVAL279
AGLY438
AGLY439
AGLU440
A1HZ701
AHOH814
BSER575
BHOH801
BHOH802
BHOH803
BHOH860

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. FQLSGGTTGtPK
ChainResidueDetails
APHE187-LYS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22365602
ChainResidueDetails
BASN235
BALA335
AALA335
AASN235

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23897471
ChainResidueDetails
BLYS432
BLYS441
ASER240
ALYS432
ALYS441
BSER240

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22365602, ECO:0000269|PubMed:23897471
ChainResidueDetails
AGLY309
AASP415
BGLY309
BVAL331
BASP415
AVAL331

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16632253, ECO:0007744|PDB:2FQ1
ChainResidueDetails
AASP574
BASP557
BGLY572
BASP574
AASP557
AGLY572

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000269|PubMed:22365602, ECO:0007744|PDB:3RG2
ChainResidueDetails
ASER575
BSER575

221051

PDB entries from 2024-06-12

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