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4ZLA

Bestatin complex structure of leucine aminopeptidase from Helicobacter pylori

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0019538biological_processprotein metabolic process
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008235molecular_functionmetalloexopeptidase activity
B0019538biological_processprotein metabolic process
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
C0004177molecular_functionaminopeptidase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008235molecular_functionmetalloexopeptidase activity
C0019538biological_processprotein metabolic process
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
C0070006molecular_functionmetalloaminopeptidase activity
D0004177molecular_functionaminopeptidase activity
D0005737cellular_componentcytoplasm
D0006508biological_processproteolysis
D0008235molecular_functionmetalloexopeptidase activity
D0019538biological_processprotein metabolic process
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
D0070006molecular_functionmetalloaminopeptidase activity
E0004177molecular_functionaminopeptidase activity
E0005737cellular_componentcytoplasm
E0006508biological_processproteolysis
E0008235molecular_functionmetalloexopeptidase activity
E0019538biological_processprotein metabolic process
E0030145molecular_functionmanganese ion binding
E0046872molecular_functionmetal ion binding
E0070006molecular_functionmetalloaminopeptidase activity
F0004177molecular_functionaminopeptidase activity
F0005737cellular_componentcytoplasm
F0006508biological_processproteolysis
F0008235molecular_functionmetalloexopeptidase activity
F0019538biological_processprotein metabolic process
F0030145molecular_functionmanganese ion binding
F0046872molecular_functionmetal ion binding
F0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue ZN A 501
ChainResidue
ALYS258
AASP263
AASP281
AGLU342
AZN502
ABCT504
ABES505

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 502
ChainResidue
AGLU342
AZN501
ABES505
AASP263
AASP340

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
AALA461
AGLY462
ATYR465
AHOH611
AHOH627
AHOH912

site_idAC4
Number of Residues8
Detailsbinding site for residue BCT A 504
ChainResidue
ALYS258
AALA341
AGLU342
AGLY343
AARG344
ALEU368
AZN501
ABES505

site_idAC5
Number of Residues19
Detailsbinding site for residue BES A 505
ChainResidue
ALYS258
AASP263
ALYS270
AASP281
AASP340
AGLU342
ATHR367
ALEU368
ATHR369
AGLY370
AILE428
AALA461
AZN501
AZN502
ABCT504
AHOH604
AHOH614
AHOH747
AHOH836

site_idAC6
Number of Residues7
Detailsbinding site for residue ZN B 501
ChainResidue
BLYS258
BASP263
BASP281
BGLU342
BZN502
BBCT504
BBES505

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN B 502
ChainResidue
BASP263
BASP340
BGLU342
BZN501
BBES505

site_idAC8
Number of Residues6
Detailsbinding site for residue NA B 503
ChainResidue
BALA461
BGLY462
BTYR465
BHOH647
BHOH681
BHOH931

site_idAC9
Number of Residues8
Detailsbinding site for residue BCT B 504
ChainResidue
BLYS258
BALA341
BGLU342
BGLY343
BARG344
BLEU368
BZN501
BBES505

site_idAD1
Number of Residues17
Detailsbinding site for residue BES B 505
ChainResidue
BLYS258
BASP263
BLYS270
BASP281
BASP340
BGLU342
BTHR367
BLEU368
BTHR369
BGLY370
BALA461
BZN501
BZN502
BBCT504
BHOH733
BHOH754
BHOH765

site_idAD2
Number of Residues7
Detailsbinding site for residue ZN C 501
ChainResidue
CLYS258
CASP263
CASP281
CGLU342
CZN502
CBCT504
CBES505

site_idAD3
Number of Residues5
Detailsbinding site for residue ZN C 502
ChainResidue
CBES505
CASP263
CASP340
CGLU342
CZN501

site_idAD4
Number of Residues6
Detailsbinding site for residue NA C 503
ChainResidue
CALA461
CGLY462
CTYR465
CHOH2562
CHOH2571
CHOH2787

site_idAD5
Number of Residues8
Detailsbinding site for residue BCT C 504
ChainResidue
CLYS258
CALA341
CGLU342
CGLY343
CARG344
CLEU368
CZN501
CBES505

site_idAD6
Number of Residues18
Detailsbinding site for residue BES C 505
ChainResidue
CLYS258
CASP263
CLYS270
CASP281
CASP340
CGLU342
CTHR367
CLEU368
CTHR369
CGLY370
CALA461
CZN501
CZN502
CBCT504
CHOH2543
CHOH2601
CHOH2615
CHOH2787

site_idAD7
Number of Residues7
Detailsbinding site for residue ZN D 501
ChainResidue
DLYS258
DASP263
DASP281
DGLU342
DZN502
DBCT504
DBES505

site_idAD8
Number of Residues5
Detailsbinding site for residue ZN D 502
ChainResidue
DASP263
DASP340
DGLU342
DZN501
DBES505

site_idAD9
Number of Residues6
Detailsbinding site for residue NA D 503
ChainResidue
DALA461
DGLY462
DTYR465
DHOH618
DHOH692
DHOH935

site_idAE1
Number of Residues8
Detailsbinding site for residue BCT D 504
ChainResidue
DLYS258
DALA341
DGLU342
DGLY343
DARG344
DLEU368
DZN501
DBES505

site_idAE2
Number of Residues15
Detailsbinding site for residue BES D 505
ChainResidue
DLYS258
DASP263
DLYS270
DASP281
DASP340
DGLU342
DTHR367
DLEU368
DTHR369
DGLY370
DALA461
DZN501
DZN502
DBCT504
DHOH653

site_idAE3
Number of Residues7
Detailsbinding site for residue ZN E 501
ChainResidue
ELYS258
EASP263
EASP281
EGLU342
EZN502
EBCT504
EBES505

site_idAE4
Number of Residues5
Detailsbinding site for residue ZN E 502
ChainResidue
EASP263
EASP340
EGLU342
EZN501
EBES505

site_idAE5
Number of Residues6
Detailsbinding site for residue NA E 503
ChainResidue
EALA461
EGLY462
ETYR465
EHOH634
EHOH856
EHOH923

site_idAE6
Number of Residues8
Detailsbinding site for residue BCT E 504
ChainResidue
ELYS258
EALA341
EGLU342
EGLY343
EARG344
ELEU368
EZN501
EBES505

site_idAE7
Number of Residues16
Detailsbinding site for residue BES E 505
ChainResidue
ELYS258
EASP263
ELYS270
EMET278
EASP281
EASP340
EGLU342
ETHR367
ELEU368
ETHR369
EGLY370
EILE428
EZN501
EZN502
EBCT504
EHOH632

site_idAE8
Number of Residues7
Detailsbinding site for residue ZN F 501
ChainResidue
FLYS258
FASP263
FASP281
FGLU342
FZN502
FBCT504
FBES505

site_idAE9
Number of Residues5
Detailsbinding site for residue ZN F 502
ChainResidue
FASP263
FASP340
FGLU342
FZN501
FBES505

site_idAF1
Number of Residues6
Detailsbinding site for residue NA F 503
ChainResidue
FALA461
FGLY462
FTYR465
FHOH614
FHOH878
FHOH919

site_idAF2
Number of Residues8
Detailsbinding site for residue BCT F 504
ChainResidue
FLYS258
FALA341
FGLU342
FGLY343
FARG344
FLEU368
FZN501
FBES505

site_idAF3
Number of Residues15
Detailsbinding site for residue BES F 505
ChainResidue
FLYS258
FASP263
FLYS270
FASP281
FASP340
FGLU342
FTHR367
FLEU368
FTHR369
FGLY370
FALA461
FZN501
FZN502
FBCT504
FHOH625

Functional Information from PROSITE/UniProt
site_idPS00631
Number of Residues8
DetailsCYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL
ChainResidueDetails
AASN338-LEU345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
ALYS270
AARG344
BLYS270
BARG344
CLYS270
CARG344
DLYS270
DARG344
ELYS270
EARG344
FLYS270
FARG344

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
EGLU342
FLYS258
FASP263
FASP281
FASP340
FGLU342
ALYS258
AASP263
AASP281
AASP340
AGLU342
BLYS258
BASP263
BASP281
BASP340
BGLU342
CLYS258
CASP263
CASP281
CASP340
CGLU342
DLYS258
DASP263
DASP281
DASP340
DGLU342
ELYS258
EASP263
EASP281
EASP340

221051

PDB entries from 2024-06-12

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