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4DZ2

Crystal structure of a Peptidyl-prolyl cis-trans isomerase with surface mutation R92G 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
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FK5 A 200
ChainResidue
ATYR33
ATYR89
AILE98
APHE106
AHOH383
AHOH389
AHOH403
BGLY60
BMET61
BFK5200
APHE43
AASP44
APHE53
AMET61
AVAL62
AILE63
ATRP66
AGLY88

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 201
ChainResidue
AASP51
APRO52
AASP112
AVAL113
AHOH369
AHOH370

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FK5 B 200
ChainResidue
AGLY60
AMET61
AFK5200
BTYR33
BPHE43
BASP44
BARG49
BPHE53
BMET61
BVAL62
BILE63
BTRP66
BGLY88
BTYR89
BPHE106
BHOH359
BHOH391
BHOH403

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BASP51
BPRO52
BASP112
BVAL113
BHOH364
BHOH365

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PDB entries from 2024-07-24

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