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6LKB

Crystal Structure of the peptidylprolyl isomerase domain of Arabidopsis thaliana CYP71.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 701
ChainResidue
AASP486
AHIS488
ALYS598
AHOH821
AHOH889
AHOH905
BASP486
BHOH895

site_idAC2
Number of Residues4
Detailsbinding site for residue CO A 702
ChainResidue
AASP486
BHIS481
BASP486
AHIS481

site_idAC3
Number of Residues3
Detailsbinding site for residue PO4 A 703
ChainResidue
AASP612
ALYS613
ATYR618

site_idAC4
Number of Residues3
Detailsbinding site for residue CO A 704
ChainResidue
AHIS506
AASN509
AHOH938

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 701
ChainResidue
BHIS506
BASN509
BTYR511
BHOH823
BHOH855

site_idAC6
Number of Residues5
Detailsbinding site for residue PO4 B 702
ChainResidue
BASP612
BLYS613
BTYR618
BHOH813
BHOH864

site_idAC7
Number of Residues3
Detailsbinding site for residue CO B 703
ChainResidue
BGLY599
BMET600
BASP601

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PDB entries from 2024-07-10

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