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2BB5

Structure of Human Transcobalamin in complex with Cobalamin

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 Residues29
DetailsBINDING SITE FOR RESIDUE B12 A 0
ChainResidue
AGLY85
AASN224
ATYR226
ASER227
AMET270
AGLN273
ASER357
ALEU358
ASER359
AGLY360
APRO361
AGLN86
ATYR362
ALEU363
APHE376
ATRP377
AGLN378
ALEU379
ALEU387
ALEU388
AGLY390
ATRP409
ATHR134
ASER135
ATYR137
AGLN138
AHIS172
AHIS173
AASP176

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE B12 B 410
ChainResidue
BGLY85
BGLN86
BTHR134
BTYR137
BGLN138
BHIS172
BHIS173
BASP176
BASN224
BTYR226
BSER227
BMET270
BGLN273
BSER357
BLEU358
BSER359
BGLY360
BPRO361
BTYR362
BLEU363
BPHE376
BTRP377
BLEU379
BLEU387
BLEU388
BGLY390
BTRP409
BHOH414

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16537422, ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5
ChainResidueDetails
BGLN86
BSER227
AGLN86
ASER227

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16537422, ECO:0007744|PDB:2BB5
ChainResidueDetails
BASN224
BTRP377
ATHR134
AASN224
ATRP377
BTHR134

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

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PDB entries from 2024-05-29

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