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4ZRQ

E88 deletion mutant of CD320 in complex with TC2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006824biological_processcobalt ion transport
A0009897cellular_componentexternal side of plasma membrane
A0015889biological_processcobalamin transport
A0031419molecular_functioncobalamin binding
A0043202cellular_componentlysosomal lumen
A0046872molecular_functionmetal ion binding
A0140355molecular_functioncargo receptor ligand activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006824biological_processcobalt ion transport
B0009897cellular_componentexternal side of plasma membrane
B0015889biological_processcobalamin transport
B0031419molecular_functioncobalamin binding
B0043202cellular_componentlysosomal lumen
B0046872molecular_functionmetal ion binding
B0140355molecular_functioncargo receptor ligand activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue CNC A 501
ChainResidue
AGLY85
AMET270
AGLN273
ASER357
ALEU358
ASER359
AGLY360
APRO361
ATYR362
ALEU363
APHE376
AGLN86
ATRP377
AGLN378
ALEU379
ALEU387
ALEU388
AGLY390
ATRP409
AHOH605
ATHR134
ATYR137
AGLN138
AASP176
AASN224
ATYR226
ASER227

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 502
ChainResidue
ASER174
ATHR177
ATRP409
AHOH609
AHOH610

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
AHIS169
AHIS172
AHIS173
AGLU211
AHOH612

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
AGLY372
AGLU373
AGLU375
BGLY372
BGLU375

site_idAC5
Number of Residues28
Detailsbinding site for residue CNC B 501
ChainResidue
BGLY85
BGLN86
BTHR134
BTYR137
BGLN138
BASP176
BASN224
BTYR226
BSER227
BMET270
BGLN273
BSER357
BLEU358
BSER359
BGLY360
BPRO361
BTYR362
BLEU363
BPHE376
BTRP377
BGLN378
BLEU379
BLEU387
BLEU388
BGLY390
BTRP409
BHOH606
BHOH607

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL B 502
ChainResidue
BGLN63
BARG102
BGLY103
BLYS105
DASP77
DLEU78
DASP79

site_idAC7
Number of Residues6
Detailsbinding site for residue CA C 201
ChainResidue
CTRP150
CASP153
CHIS155
CASP157
CASP163
CGLU164

site_idAC8
Number of Residues6
Detailsbinding site for residue CA C 202
ChainResidue
CTRP72
CCYS74
CASP75
CASP77
CASP79
CASP85

site_idAC9
Number of Residues6
Detailsbinding site for residue CA D 201
ChainResidue
DTRP150
DASP153
DHIS155
DASP157
DASP163
DGLU164

site_idAD1
Number of Residues5
Detailsbinding site for residue CA D 202
ChainResidue
DASP85
DTRP72
DASP75
DASP77
DASP79

Functional Information from PROSITE/UniProt
site_idPS00468
Number of Residues14
DetailsCOBALAMIN_BINDING Eukaryotic cobalamin-binding proteins signature. SVDTAAMAgLAFTC
ChainResidueDetails
ASER174-CYS187

site_idPS01209
Number of Residues27
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CVpltwr.CDrdlDCsdgsDEEcriepC
ChainResidueDetails
CCYS67-CYS94
CCYS145-CYS167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:27411955, ECO:0007744|PDB:4ZRP
ChainResidueDetails
CTRP72
CCYS158
CGLU164
CLEU165
DTRP72
DASP75
DASP77
DASP79
DASP85
DGLU87
DARG151
CASP75
DGLY154
DPRO156
DCYS158
DGLU164
DLEU165
CASP77
CASP79
CASP85
CGLU87
CARG151
CGLY154
CPRO156

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CCYS127
DCYS127
ATRP377
BTHR134
BASN224
BTRP377

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS172
BHIS172

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16537422
ChainResidueDetails
AGLN273
BGLN273

224004

PDB entries from 2024-08-21

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