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1W61

proline racemase in complex with 2 molecules of pyrrole-2-carboxylic acid (holo form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0018112molecular_functionproline racemase activity
A0047580molecular_function4-hydroxyproline epimerase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0018112molecular_functionproline racemase activity
B0047580molecular_function4-hydroxyproline epimerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYC A 700
ChainResidue
ALEU127
ACYS130
AGLY131
AHIS132
APHE290
AASP296
ACYS300
AGLY301
ATHR302

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYC B 700
ChainResidue
BLEU127
BCYS130
BGLY131
BHIS132
BPHE290
BASP296
BCYS300
BGLY301
BTHR302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ACYS130
BCYS130

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
ACYS300
BCYS300

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY131
AASP296
AGLY301
BGLY131
BASP296
BGLY301

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN183
AASN236
AASN252
BASN183
BASN236
BASN252

222415

PDB entries from 2024-07-10

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