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6O49

CRYSTAL STRUCTURE OF SMT FUSION PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM BURKHOLDERIA PSEUDOMALLEI COMPLEXED WITH SF339

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 LL7 A 201
ChainResidue
ATYR33
AALA94
AGLY95
AVAL97
APHE106
AHOH303
AHOH349
AHOH433
AHOH455
BLL7201
APHE43
AASP44
APHE53
AMET61
AVAL62
AILE63
ATRP66
ATYR89

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 202
ChainResidue
AASP51
APRO52
AHOH395
BASP51
BPRO52
BHOH372

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 203
ChainResidue
AGLY58
AASP67
AGLU68
AGLN71
AHOH310
AHOH336
AHOH342
AHOH370

site_idAC4
Number of Residues17
Detailsbinding site for residue LL7 B 201
ChainResidue
ALL7201
AHOH303
BTYR33
BPHE43
BASP44
BPHE53
BVAL62
BILE63
BTRP66
BTYR89
BGLY95
BVAL97
BILE98
BPHE106
BHOH312
BHOH363
BHOH375

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 202
ChainResidue
AHOH414
AHOH449
BASP112
BVAL113
BHOH304
BHOH318

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO B 203
ChainResidue
BGLN86
BGLY88
BGLY90
BHOH301
BHOH398

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO B 204
ChainResidue
BARG92
BHOH333
BHOH431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
AGLY0
BGLY0

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PDB entries from 2024-07-17

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