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1RTM

TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
10001867biological_processcomplement activation, lectin pathway
10005537molecular_functionmannose binding
20001867biological_processcomplement activation, lectin pathway
20005537molecular_functionmannose binding
30001867biological_processcomplement activation, lectin pathway
30005537molecular_functionmannose binding
Functional Information from PDB Data
site_id11
Number of Residues7
Details
ChainResidue
1CA1
1ASP161
1GLU165
1ASP188
1GLU193
1ASP194
1HOH235

site_id12
Number of Residues7
Details
ChainResidue
2GLU165
2ASP188
2GLU193
2ASP194
2HOH243
2CA1
2ASP161

site_id13
Number of Residues7
Details
ChainResidue
3CA1
3ASP161
3GLU165
3ASP188
3GLU193
3ASP194
3HOH238

site_id21
Number of Residues7
Details
ChainResidue
1CA2
1GLU185
1ASN187
1GLU193
1ASN205
1ASP206
1GOL222

site_id22
Number of Residues7
Details
ChainResidue
2CA2
2GLU185
2ASN187
2GLU193
2ASN205
2ASP206
2GOL222

site_id23
Number of Residues7
Details
ChainResidue
3CA2
3GLU185
3ASN187
3GLU193
3ASN205
3ASP206
3GOL222

site_id31
Number of Residues7
Details
ChainResidue
1CA3
1GLU165
1ASP194
1HOH233
1HOH234
1GOL10
1GLU84

site_id32
Number of Residues5
Details
ChainResidue
2CA3
2GLU165
2ASP194
2HOH233
2HOH234

site_id33
Number of Residues7
Details
ChainResidue
3CA3
3GLU165
3ASP194
3HOH225
1HOH227
3HOH333
3GLU84

site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 1
ChainResidue
1ASP161
1GLU165
1ASP188
1GLU193
1ASP194
1HOH235

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 2
ChainResidue
1GLU185
1ASN187
1GLU193
1ASN205
1ASP206
1GOL222

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 3
ChainResidue
1GOL10
1GLU84
1GLU165
1ASP194
1HOH233
1HOH234

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL 1 4
ChainResidue
1ASP194
1CYS209

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 2 1
ChainResidue
2ASP161
2GLU165
2ASP188
2GLU193
2ASP194
2HOH243

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 2 2
ChainResidue
2GLU185
2ASN187
2GLU193
2ASN205
2ASP206
2GOL222

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA 2 3
ChainResidue
2GLU165
2ASP194
2HOH233
2HOH234

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL 2 4
ChainResidue
2CYS209
2ASP194
2SER208

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 1
ChainResidue
3ASP161
3GLU165
3ASP188
3GLU193
3ASP194
3HOH238

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 2
ChainResidue
3GLU185
3ASN187
3GLU193
3ASN205
3ASP206
3GOL222

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 3
ChainResidue
1HOH227
3GLU84
3GLU165
3ASP194
3HOH225
3HOH333

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL 3 4
ChainResidue
3ASP194
3CYS209
3HOH322

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL 1 222
ChainResidue
1CA2
1GOL13
1GLU185
1ASN187
1GLU193
1ASN205
1ASP206
1ILE207

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL 2 222
ChainResidue
2CA2
2GLU185
2ASN187
2HIS189
2GLU193
2ASN205
2ASP206
2ILE207

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL 3 222
ChainResidue
3CA2
3GLU185
3ASN187
3GLU193
3ASN205
3ASP206
3ILE207
3HOH349

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL 1 223
ChainResidue
1GOL15
1PHE111
1PHE219
1HOH254
1HOH311
1HOH359

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL 2 5
ChainResidue
1LEU98
2ASN96
2PHE111
2HOH226
2HOH298
2HOH335

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL 3 6
ChainResidue
3ASN96
3PHE111
3PHE219
3HOH231
3HOH309
3HOH328

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL 1 7
ChainResidue
1LYS125
1CYS128
1SER129
1THR134
1VAL135
1VAL171

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL 2 8
ChainResidue
2LYS97
2ALA100
2PHE101
2LYS105
2HOH227
2HOH315
2HOH335

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL 1 9
ChainResidue
1ALA83
1ASN86
1THR87
1GLN167
1HOH363

site_idCC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL 1 10
ChainResidue
1CA3
1ASN80
1GLU84
1ASP194
1HOH226
1HOH233
1HOH234
1HOH284
1HOH285
1HOH369
2GLU82

site_idCC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL 1 11
ChainResidue
1THR134
1PRO220
1HOH301
1HOH365
1HOH394
1HOH395
3LYS182
3LYS183
3ASP184

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL 3 12
ChainResidue
3ASN140
3ALA141
3TYR178

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL 1 13
ChainResidue
1ILE207
1GOL222
1HOH286
1HOH327

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL 1 14
ChainResidue
1LYS182
1GLU185
1VAL199
1ASN205

site_idCC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL 1 15
ChainResidue
1GLU93
1ASN96
1LYS97
1ALA100
1LYS105
1PHE111
1GOL223
1HOH274
1HOH359

Functional Information from PROSITE/UniProt
site_idPS00615
Number of Residues23
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CVtivdngl.....WNDISCqasht.AVC
ChainResidueDetails
1CYS195-CYS217

237735

PDB entries from 2025-06-18

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