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3RET

Salicylate and Pyruvate Bound Structure of the Isochorismate-Pyruvate Lyase K42E Mutant from Pseudomonas aerugionsa

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 201
ChainResidue
AARG31
BPYR301
AVAL35
AILE48
AVAL54
AMET57
ATYR86
AILE87
AGLN90
AHOH111

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR B 301
ChainResidue
AGLU42
AGLN90
AHOH111
ASAL201
BARG14
BILE17

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SAL B 201
ChainResidue
AHOH107
APYR301
BARG31
BVAL35
BILE48
BMET57
BTYR86
BILE87
BGLN90

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR A 301
ChainResidue
AARG14
AHOH107
BALA38
BALA50
BGLN90
BSAL201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG14
AGLU42
BARG14
BGLU42

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

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PDB entries from 2024-07-24

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