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SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A

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
DetailsCA SITE 1, PROTOMER 1.
ChainResidue
1CA1
1ASP161
1GLU165
1ASP188
1GLU193
1ASP194
1HOH365

site_id12
Number of Residues7
DetailsCA SITE 1, PROTOMER 2.
ChainResidue
2GLU165
2ASP188
2GLU193
2ASP194
2HOH258
2CA1
2ASP161

site_id13
Number of Residues7
DetailsCA SITE 1, PROTOMER 3.
ChainResidue
3CA1
3ASP161
3GLU165
3ASP188
3GLU193
3ASP194
3HOH294

site_id21
Number of Residues7
DetailsCA SITE 2, PROTOMER 1.
ChainResidue
1CA2
1GLU185
1ASN187
1GLU193
1ASN205
1ASP206
1HOH356

site_id22
Number of Residues7
DetailsCA SITE 2, PROTOMER 2.
ChainResidue
2CA2
2GLU185
2ASN187
2GLU193
2ASN205
2ASP206
2HOH265

site_id23
Number of Residues8
DetailsCA SITE 2, PROTOMER 3.
ChainResidue
3CA2
3GLU185
3ASN187
3GLU193
3ASN205
3ASP206
3HOH286
3HOH287

site_id31
Number of Residues6
DetailsCA SITE 3, PROTOMER 1.
ChainResidue
1CA3
1GLU165
1ASP194
1HOH366
1HOH372
1HOH373

site_id32
Number of Residues4
DetailsCA SITE 3, PROTOMER 2.
ChainResidue
2CA3
2GLU165
2ASP194
2HOH259

site_id33
Number of Residues4
DetailsCA SITE 3, PROTOMER 3.
ChainResidue
3CA3
3GLU165
3ASP194
3HOH350

site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 1
ChainResidue
1ASP161
1GLU165
1ASP188
1GLU193
1ASP194
1HOH365

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 2
ChainResidue
1GLU185
1ASN187
1GLU193
1ASN205
1ASP206
1HOH356

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 1 3
ChainResidue
1GLU84
1GLU165
1ASP194
1HOH366
1HOH372
1HOH373

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
2HOH258

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 2 2
ChainResidue
2GLU185
2ASN187
2GLU193
2ASN205
2ASP206
2HOH265

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA 2 3
ChainResidue
2GLU165
2ASP194
2HOH259

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

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 1
ChainResidue
3ASP194
3HOH294
3ASP161
3GLU165
3ASP188
3GLU193

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA 3 2
ChainResidue
3GLU185
3ASN187
3GLU193
3ASN205
3ASP206
3HOH286
3HOH287

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 3
ChainResidue
1HOH228
3GLU84
3GLU165
3ASP194
3HOH255
3HOH350

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL 3 4
ChainResidue
3ASP194
3CYS209
3HOH352

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

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PDB entries from 2024-06-12

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