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2IER

Crystal Structure of Aquifex aeolicus LpxC Complexed with Uridine 5'-Diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006796biological_processphosphate-containing compound metabolic process
A0008759molecular_functionUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
A0009245biological_processlipid A biosynthetic process
A0016787molecular_functionhydrolase activity
A0019637biological_processorganophosphate metabolic process
A0046872molecular_functionmetal ion binding
A0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
A1901135biological_processcarbohydrate derivative metabolic process
B0006796biological_processphosphate-containing compound metabolic process
B0008759molecular_functionUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
B0009245biological_processlipid A biosynthetic process
B0016787molecular_functionhydrolase activity
B0019637biological_processorganophosphate metabolic process
B0046872molecular_functionmetal ion binding
B0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AHIS79
AHIS238
AASP242
AZN606
AHOH802

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 602
ChainResidue
BHOH808
BHIS79
BHIS238
BASP242
BZN607

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 603
ChainResidue
AHIS58
AHIS200

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 604
ChainResidue
BHIS58
BHIS200

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 605
ChainResidue
AGLY2
AGLU126
BILE27
BHIS29
BGLU95

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 606
ChainResidue
AGLU78
AHIS265
AZN601
AHOH802
AHOH830

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 607
ChainResidue
BHIS58
BSER59
BGLU78
BHIS265
BZN602
BHOH808

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 608
ChainResidue
AHIS58
APLM701
AUDP801

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 609
ChainResidue
BHIS58
BPLM702
BUDP802

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE UDP A 801
ChainResidue
AHIS58
ATYR157
AGLY159
AGLU160
APHE161
AGLU197
ALYS239
AARG262
AGLY264
AHIS265
AZN608
APLM701
AHOH808
AHOH817
AHOH830
AHOH837
AHOH840

site_idBC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE UDP B 802
ChainResidue
BHIS58
BTYR157
BGLY159
BGLU160
BPHE161
BPHE194
BGLU197
BLYS239
BARG262
BGLY264
BHIS265
BZN609
BHOH810

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLM A 701
ChainResidue
AILE18
AHIS19
APHE192
AGLU197
AILE198
AGLY210
AZN608
AUDP801
AHOH843
BSER211
BLEU212
BPLM702

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PLM B 702
ChainResidue
ATYR224
APLM701
BILE18
BHIS19
BILE198
BGLY210
BSER211
BTYR224
BZN609

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AHIS85
AGLU88
ALEU153
AVAL254
ALYS255

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000305|PubMed:15705580
ChainResidueDetails
AHIS265
BHIS265

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:12819349, ECO:0000269|PubMed:15705580, ECO:0007744|PDB:1P42, ECO:0007744|PDB:1YH8, ECO:0007744|PDB:1YHC
ChainResidueDetails
AHIS79
AHIS238
AASP242
BHIS79
BHIS238
BASP242

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PDB entries from 2024-07-10

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