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2ERV

Crystal structure of the outer membrane enzyme PagL

Functional Information from GO Data
ChainGOidnamespacecontents
A0008653biological_processlipopolysaccharide metabolic process
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
A0046493biological_processlipid A metabolic process
A0050528molecular_functionacyloxyacyl hydrolase activity
B0008653biological_processlipopolysaccharide metabolic process
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0042803molecular_functionprotein homodimerization activity
B0046493biological_processlipid A metabolic process
B0050528molecular_functionacyloxyacyl hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 195
ChainResidue
AASP106
BASP106
BCXE1200

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CXE B 196
ChainResidue
BTRP25
BTRP41
BILE83

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CXE B 200
ChainResidue
BLEU132
AILE108
AALA124
BALA130

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CXE A 300
ChainResidue
ATRP25

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CXE B 400
ChainResidue
BMET15
BVAL122
BTYR142
BSER143

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CXE B 500
ChainResidue
AILE75
BGLY111

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CXE A 600
ChainResidue
AMET15
ATYR142
AHOH859

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CXE A 700
ChainResidue
AGLY111

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CXE A 800
ChainResidue
BLEU19

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CXE B 900
ChainResidue
BPHE62
BPRO64
BILE83

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CXE B 1000
ChainResidue
BVAL85
BLEU102
BPHE104
BASN129

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CXE B 1100
ChainResidue
AALA130
BILE83
BARG107
BILE108
BGLU140
BTYR142
BCXE1200

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CXE B 1200
ChainResidue
APHE104
AASP106
ASER128
ACA195
BPHE104
BASP106
BHIS126
BSER128
BCXE1100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:16632613
ChainResidueDetails
AASP2-ALA5
BALA71-GLY72
BVAL93-GLY94
BHIS126-ILE150
ATHR10
AGLU49-GLY50
AALA71-GLY72
AVAL93-GLY94
AHIS126-ILE150
BASP2-ALA5
BTHR10
BGLU49-GLY50

site_idSWS_FT_FI2
Number of Residues168
DetailsTRANSMEM: Beta stranded => ECO:0000269|PubMed:16632613
ChainResidueDetails
AALA6-ALA9
BALA6-ALA9
BGLY11-ASP26
BTHR34-TRP48
BGLY51-PHE66
BTYR68-PHE70
BASP73-ILE75
BPHE78-ARG92
BASP95-GLU105
BASN116-ILE125
AGLY11-ASP26
ATHR34-TRP48
AGLY51-PHE66
ATYR68-PHE70
AASP73-ILE75
APHE78-ARG92
AASP95-GLU105
AASN116-ILE125

site_idSWS_FT_FI3
Number of Residues34
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:16632613
ChainResidueDetails
ALYS27-SER33
AVAL67
ALYS76-PRO77
AASP106-ALA115
BLYS27-SER33
BVAL67
BLYS76-PRO77
BASP106-ALA115

site_idSWS_FT_FI4
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:15611102
ChainResidueDetails
AHIS126
ASER128
BHIS126
BSER128

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:16632613
ChainResidueDetails
AGLU140
BGLU140

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Critical for activity => ECO:0000269|PubMed:16632613
ChainResidueDetails
AASN129
BASN129

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PDB entries from 2024-07-17

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