Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4MQY

Crystal Structure of the Escherichia coli LpxC/LPC-138 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006796biological_processphosphate-containing compound metabolic process
A0008270molecular_functionzinc ion binding
A0008759molecular_functionUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
A0009245biological_processlipid A biosynthetic process
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0019637biological_processorganophosphate metabolic process
A0046872molecular_functionmetal ion binding
A0103117molecular_functionUDP-3-O-acyl-N-acetylglucosamine deacetylase activity
A1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS79
AHIS238
AASP242
A2CW402

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 2CW A 402
ChainResidue
ATHR191
APHE192
AILE198
AGLN202
AGLY210
ASER211
APHE212
AALA215
AHIS238
AASP242
AHIS265
AZN401
ASO4404
AHOH511
AHOH666
ALEU18
ALEU62
ACYS63
AGLU78
AHIS79

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 403
ChainResidue
AHOH649

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AASP59
ALYS239
AGLY264
AHIS265
A2CW402
AHOH511
AHOH553
AHOH638
AHOH666

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AGLU122
ALEU123
AASN124
AHOH587

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
ALYS22
ALYS23

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
ALYS8
AARG9
AARG204

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 408
ChainResidue
ACYS250
ATYR284

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UKW A 409
ChainResidue
AMET61
ATYR113
AMET183
ASER187
AARG188
APHE194
AASP197
ALEU201
AALA302
AHOH575
AHOH606

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000305|PubMed:15705580, ECO:0000305|PubMed:24108127
ChainResidueDetails
AHIS265

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400
ChainResidueDetails
AHIS79
AHIS238
AASP242

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon