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2H9D

Pyruvate-Bound Structure of the Isochorismate-Pyruvate Lyase 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
C0004106molecular_functionchorismate mutase activity
C0009697biological_processsalicylic acid biosynthetic process
C0016829molecular_functionlyase activity
C0016835molecular_functioncarbon-oxygen lyase activity
C0016853molecular_functionisomerase activity
C0019752biological_processcarboxylic acid metabolic process
C0042864biological_processpyochelin biosynthetic process
C0043904molecular_functionisochorismate pyruvate lyase activity
C0046417biological_processchorismate metabolic process
D0004106molecular_functionchorismate mutase activity
D0009697biological_processsalicylic acid biosynthetic process
D0016829molecular_functionlyase activity
D0016835molecular_functioncarbon-oxygen lyase activity
D0016853molecular_functionisomerase activity
D0019752biological_processcarboxylic acid metabolic process
D0042864biological_processpyochelin biosynthetic process
D0043904molecular_functionisochorismate pyruvate lyase activity
D0046417biological_processchorismate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 301
ChainResidue
AGLU15
AASP18
CHOH238
DGLU15
DASP18
DHOH343

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR C 201
ChainResidue
DLYS42
DGLN90
DPYR202
CARG14
CHOH211
DALA38

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR D 202
ChainResidue
CPYR201
CHOH211
DARG31
DMET57
DTYR86
DILE87
DGLN90

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR C 203
ChainResidue
CARG31
CARG53
CMET57
CTYR86
CILE87
CPYR206
CHOH249

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PYR B 204
ChainResidue
BARG31
BPRO49
BMET57
BILE83
BGLN90

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR A 205
ChainResidue
AARG31
AVAL35
AMET57
ATYR86
AILE87
AHOH214

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PYR C 206
ChainResidue
CLYS42
CARG53
CGLN90
CPYR203
DARG14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG14
ALYS42
BARG14
BLYS42
CARG14
CLYS42
DARG14
DLYS42

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG31
AGLN90
BARG31
BGLN90
CARG31
CGLN90
DARG31
DGLN90

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PDB entries from 2024-06-12

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