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1JRG

Crystal Structure of the R3 form of Pectate Lyase A, Erwinia chrysanthemi

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0030570molecular_functionpectate lyase activity
A0045490biological_processpectin catabolic process
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0016829molecular_functionlyase activity
B0030570molecular_functionpectate lyase activity
B0045490biological_processpectin catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AARG244
AARG246
AGLY275
ATHR276
APHE304
AASN305

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BTHR276
BPHE304
BASN305
BARG244
BARG246
BGLY275

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AGLU240
AARG241
AARG244
ATYR270
APHE304

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1004
ChainResidue
BGLU240
BARG241
BARG244
BTYR270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AGLU240
BGLU240
AARG241
BARG241

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11073
ChainResidueDetails
AALA141
ATRP143
AHIS183
ALEU187
BALA141
BTRP143
BHIS183
BLEU187

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU142
AASP144
AASP184
AASP188
BGLU142
BASP144
BASP184
BASP188

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2pec
ChainResidueDetails
AASP144
AARG241

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2pec
ChainResidueDetails
BASP144
BARG241

222036

PDB entries from 2024-07-03

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