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1Q6I

Crystal structure of a truncated form of FkpA from Escherichia coli, in complex with immunosuppressant FK506

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
A0016853molecular_functionisomerase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042026biological_processprotein refolding
A0042597cellular_componentperiplasmic space
A0044183molecular_functionprotein folding chaperone
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
B0016853molecular_functionisomerase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042026biological_processprotein refolding
B0042597cellular_componentperiplasmic space
B0044183molecular_functionprotein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FK5 A 301
ChainResidue
ATYR146
AHOH329
AHOH365
AHOH389
AHOH416
AHOH418
AHOH420
BLYS48
BLYS51
BHOH429
APHE156
AASP157
AVAL173
AILE174
ATRP177
ATYR200
AILE208
APHE216

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FK5 B 401
ChainResidue
BTYR146
BPHE156
BASP157
BARG162
BLEU166
BGLY172
BVAL173
BILE174
BTRP177
BALA199
BTYR200
BILE208
BHOH491

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
ATYR200
AILE174
AASP157

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
BTYR200
BILE174
BASP157

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PDB entries from 2026-01-28

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