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4P9W

Structure of ConA/Rh3Man

Functional Information from GO Data
ChainGOidnamespacecontents
A0005537molecular_functionD-mannose binding
A0006952biological_processdefense response
A0030246molecular_functioncarbohydrate binding
A0046872molecular_functionmetal ion binding
A0050688biological_processregulation of defense response to virus
B0005537molecular_functionD-mannose binding
B0006952biological_processdefense response
B0030246molecular_functioncarbohydrate binding
B0046872molecular_functionmetal ion binding
B0050688biological_processregulation of defense response to virus
C0005537molecular_functionD-mannose binding
C0006952biological_processdefense response
C0030246molecular_functioncarbohydrate binding
C0046872molecular_functionmetal ion binding
C0050688biological_processregulation of defense response to virus
D0005537molecular_functionD-mannose binding
D0006952biological_processdefense response
D0030246molecular_functioncarbohydrate binding
D0046872molecular_functionmetal ion binding
D0050688biological_processregulation of defense response to virus
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue R3M A 301
ChainResidue
ATYR12
AHOH426
BR3M301
AASN14
AASP16
AGLY98
ALEU99
ATYR100
AALA207
AASP208
AARG228

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 302
ChainResidue
AGLU8
AASP10
AASP19
AHIS24
AHOH413
AHOH414

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AASP10
ATYR12
AASN14
AASP19
AHOH415
AHOH416

site_idAC4
Number of Residues13
Detailsbinding site for residue R3M B 301
ChainResidue
ATYR100
AHIS205
AR3M301
AHOH405
BTYR12
BASN14
BGLY98
BLEU99
BTYR100
BALA207
BASP208
BGLY227
BARG228

site_idAC5
Number of Residues6
Detailsbinding site for residue MN B 302
ChainResidue
BGLU8
BASP10
BASP19
BHIS24
BHOH406
BHOH407

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BASP10
BTYR12
BASN14
BASP19
BHOH408
BHOH409

site_idAC7
Number of Residues13
Detailsbinding site for residue R3M C 301
ChainResidue
CTYR12
CASN14
CASP16
CGLY98
CLEU99
CTYR100
CALA207
CASP208
CGLY227
CARG228
CHOH424
DLEU99
DR3M301

site_idAC8
Number of Residues6
Detailsbinding site for residue MN C 302
ChainResidue
CGLU8
CASP10
CASP19
CHIS24
CHOH405
CHOH406

site_idAC9
Number of Residues6
Detailsbinding site for residue CA C 303
ChainResidue
CASP10
CTYR12
CASN14
CASP19
CHOH407
CHOH408

site_idAD1
Number of Residues13
Detailsbinding site for residue R3M D 301
ChainResidue
CTYR100
CHIS205
CR3M301
DTYR12
DASN14
DGLY98
DLEU99
DTYR100
DALA207
DASP208
DGLY227
DARG228
DHOH401

site_idAD2
Number of Residues6
Detailsbinding site for residue MN D 302
ChainResidue
DGLU8
DASP10
DASP19
DHIS24
DHOH403
DHOH408

site_idAD3
Number of Residues6
Detailsbinding site for residue CA D 303
ChainResidue
DASP10
DTYR12
DASN14
DASP19
DHOH402
DHOH410

Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT
ChainResidueDetails
AVAL5-THR11

site_idPS00308
Number of Residues10
DetailsLECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS
ChainResidueDetails
ALEU85-SER94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P81461","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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