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4LAW

Crystal Structure Analysis of FKBP52, Crystal Form III

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 301
ChainResidue
AGLU110
ASER115

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 302
ChainResidue
AARG157
AGLY158
ATYR161
AGLU212

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 303
ChainResidue
AARG206
AGLN209
AGLU166
ATYR202
AGLU205

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 304
ChainResidue
AVAL86
AILE87
ATYR113
APHE130

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 305
ChainResidue
AVAL99
APHE137

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 301
ChainResidue
BPHE54
BGLU136
BTYR220

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 302
ChainResidue
BPHE77
BVAL86
BILE87
BTYR113

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS B 303
ChainResidue
BGLU166
BGLY193
BTYR202
BGLU205
BARG206
BGLN209

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 304
ChainResidue
AARG189
AGLU191
BPRO124
BHOH409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000250|UniProtKB:P27124
ChainResidueDetails
ATHR143
BTHR143

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR220
BTYR220

227344

PDB entries from 2024-11-13

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