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4K7G

Crystal structure of a 3-hydroxyproline dehydratse from agrobacterium vitis, target efi-506470, with bound pyrrole 2-carboxylate, ordered active site

Functional Information from GO Data
ChainGOidnamespacecontents
B0016829molecular_functionlyase activity
B0047580molecular_function4-hydroxyproline epimerase activity
B0050346molecular_functiontrans-L-3-hydroxyproline dehydratase activity
D0016829molecular_functionlyase activity
D0047580molecular_function4-hydroxyproline epimerase activity
D0050346molecular_functiontrans-L-3-hydroxyproline dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT B 901
ChainResidue
BALA152
BHOH1151
BHOH1158
BHOH1159
BHOH1204
BTHR164
BASP166
BILE176
BVAL177
BASP178
BTHR228
BARG270
BHOH1085

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT B 902
ChainResidue
BASP85
BPRO88
BASP172
BSER173
BTRP219
BASN220
BHIS221
BSER223
BHOH1317

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT B 903
ChainResidue
DALA152
DTHR164
DASP166
DILE176
DVAL177
DASP178
DTHR228
DARG270
DHOH596
DHOH622
DHOH665

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYC B 904
ChainResidue
BGLU17
BSER90
BGLY91
BSER92
BASP252
BTHR256
BGLY257
BTHR258

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYC D 401
ChainResidue
DGLU17
DHIS62
DGLU82
DSER90
DGLY91
DSER92
DASP252
DTHR256
DGLY257
DTHR258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:24980702
ChainResidueDetails
BSER90
DSER90

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:24980702
ChainResidueDetails
BGLY91
BASP252
BGLY257
DGLY91
DASP252
DGLY257

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PDB entries from 2024-10-30

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