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2H9C

Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa

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 Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 100
ChainResidue
AARG31
AARG53
AMET57
AILE83
ATYR86
BILE17

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 100
ChainResidue
BHOH101
BARG31
BPRO49
BMET57

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 101
ChainResidue
AGLN26
BGLY9
BALA11
BASP12
BGLU67
BASN68

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 102
ChainResidue
ALYS36
AALA37
AARG40
AHOH120
BPRO4
BGLU5

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 103
ChainResidue
AGLN26
AARG30
BLYS2
BTHR8

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:21751784
ChainResidueDetails
AARG14
ALYS42
BARG14
BLYS42

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 Residues2
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
AARG14
BARG31

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ecm
ChainResidueDetails
AARG31
BARG14

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PDB entries from 2024-11-06

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