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3HGX

Crystal Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase K42A mutant in complex with salicylate and pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004106molecular_functionchorismate mutase activity
A0009697biological_processsalicylic acid biosynthetic process
A0016829molecular_functionlyase activity
A0016835molecular_functioncarbon-oxygen lyase activity
A0016853molecular_functionisomerase activity
A0019752biological_processcarboxylic acid metabolic process
A0042864biological_processpyochelin biosynthetic process
A0043904molecular_functionisochorismate pyruvate lyase activity
A0046417biological_processchorismate metabolic process
B0004106molecular_functionchorismate mutase activity
B0009697biological_processsalicylic acid biosynthetic process
B0016829molecular_functionlyase activity
B0016835molecular_functioncarbon-oxygen lyase activity
B0016853molecular_functionisomerase activity
B0019752biological_processcarboxylic acid metabolic process
B0042864biological_processpyochelin biosynthetic process
B0043904molecular_functionisochorismate pyruvate lyase activity
B0046417biological_processchorismate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SAL A 101
ChainResidue
AARG31
BHOH107
AVAL35
AILE48
APRO49
AMET57
ATYR86
AILE87
AGLN90
BPYR102

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PYR B 102
ChainResidue
AALA38
AARG53
AGLN90
BARG14
BHOH107

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR A 103
ChainResidue
AARG14
AILE17
BALA38
BARG53
BGLN90
BSAL104

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SAL B 104
ChainResidue
APYR103
BARG31
BVAL35
BILE48
BPRO49
BMET57
BTYR86
BILE87
BGLN90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG14
AALA42
BARG14
BALA42

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG31
AGLN90
BARG31
BGLN90

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
AARG31

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
BARG31

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
AARG14

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
BARG14

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PDB entries from 2024-10-16

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