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3WOO

Crystal structure of the DAP BII hexapeptide complex I

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008239molecular_functiondipeptidyl-peptidase activity
A0009056biological_processcatabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0051603biological_processproteolysis involved in protein catabolic process
A0070009molecular_functionserine-type aminopeptidase activity
B0004175molecular_functionendopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0006508biological_processproteolysis
B0008239molecular_functiondipeptidyl-peptidase activity
B0009056biological_processcatabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0051603biological_processproteolysis involved in protein catabolic process
B0070009molecular_functionserine-type aminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
ATHR598
BHOH965
APHE600
AILE639
AHOH919
AHOH1053
AHOH1125
AHOH1410
BASP593
BGLY594

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 802
ChainResidue
AASP59
ALYS251
AHIS252
ATRP253
ALYS255
AHOH1219

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 803
ChainResidue
AGLY68
AARG175
AHOH952
AHOH1208
AHOH1283
AHOH1357

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 804
ChainResidue
ATYR89
ALYS208
AASP212
AALA322
AALA326
AASN329
AHOH1439

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
ACYS87
AALA88
AGLY90
AALA91
ATYR228
AHOH944
AHOH1026
AHOH1032
AHOH1157

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 806
ChainResidue
AARG413
ALEU535
AGLU539
AARG542
AHOH1099
AHOH1195
AHOH1396

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 807
ChainResidue
AASN101
AGLN318

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 808
ChainResidue
AALA257
AASP258
AARG699
AHOH920
AHOH1311

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 809
ChainResidue
ALYS47
AGLU635
AHIS665
AHOH1436

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 810
ChainResidue
AGLU505
ALYS508
AHOH1433
BGLU438

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 801
ChainResidue
AASP593
AGLY594
AHOH945
BTHR598
BPHE600
BILE639
BHOH942
BHOH1131

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 802
ChainResidue
BLEU127
BASP128
BPHE172
BLEU191
BLYS251

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 803
ChainResidue
BASP59
BLYS251
BHIS252
BTRP253
BLYS255
BPRO468

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 804
ChainResidue
BGLY68
BARG175
BASN190
BHOH955

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 805
ChainResidue
BLYS47
BGLU635
BHIS665
BHOH1295

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 806
ChainResidue
AGLU438
BGLU505
BLYS508
BHOH1294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749
ChainResidueDetails
AALA86
AASP224
ASER657
BALA86
BASP224
BSER657

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24827749
ChainResidueDetails
AASN215
AASN330
AGLY655
APHE673
BASN215
BASN330
BGLY655
BPHE673

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PDB entries from 2024-10-30

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