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3UQA

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation A54E from Burkholderia pseudomallei complexed with FK506

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FK5 A 114
ChainResidue
AGLY26
AILE63
ATRP66
AGLY88
ATYR89
APHE106
AHOH202
AHOH203
ATYR33
APHE43
AASP44
APHE53
AGLY59
AMET61
AMET61
AVAL62

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 115
ChainResidue
AGLY26
AGLN27
ATHR28
AASN50
AVAL113

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 116
ChainResidue
AASP-23
AARG-27
AARG-52
AHOH120
AHOH143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
AGLY0

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PDB entries from 2024-07-24

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