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4MSP

Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0046872molecular_functionmetal ion binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 201
ChainResidue
AASP129
AASN131
AASP133
ALYS135
AGLU140
AHOH345

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 202
ChainResidue
APHE179
AGLU184
AHOH358
AASP173
AASP175
AASP177

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 203
ChainResidue
AGLU172
AGLU184
ATYR187
AHIS189

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE A 204
ChainResidue
ALEU145
AHIS152
APGO206
BLEU145
BGLU148
BHIS152

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 205
ChainResidue
AALA89
AGLY93
ALYS94
AGLU95
AGLU103

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO A 206
ChainResidue
AHIS152
AGLY153
AALA154
A1PE204
BLYS188

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO A 207
ChainResidue
APRO16
APHE17
ACYS19
BASP132

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 208
ChainResidue
AHIS32
ATYR33
AHIS48
ALYS81
AASN109
AHOH383

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BASP129
BASN131
BASP133
BLYS135
BGLU140
BHOH308

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP173
BASP175
BASP177
BPHE179
BGLU184
BHOH428

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO B 203
ChainResidue
AARG120
ASER124
APHE185
BHIS152

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO B 204
ChainResidue
ATRP57
AARG116
BILE115
BHOH316
BHOH392

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGO B 205
ChainResidue
BHIS20
BHOH338

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGO B 206
ChainResidue
BVAL12
BHOH423

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGO B 207
ChainResidue
AILE56
ATRP57
AHOH313
AHOH320
BLEU28
BTRP57
BARG116

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. HDEL
ChainResidueDetails
AHIS189-LEU192

site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DEDKDGFISarEF
ChainResidueDetails
AASP173-PHE185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:24272907, ECO:0000305|PubMed:24821723, ECO:0007744|PDB:4MSP
ChainResidueDetails
AASP129
BLYS135
BGLU140
BPHE179
AASN131
AASP133
ALYS135
AGLU140
APHE179
BASP129
BASN131
BASP133

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:24272907, ECO:0000305|PubMed:24821723, ECO:0007744|PDB:4MSP
ChainResidueDetails
AASP173
AASP175
AASP177
AGLU184
BASP173
BASP175
BASP177
BGLU184

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN157
BASN157

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PDB entries from 2024-07-17

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