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6G8B

E. coli Aminopeptidase N solved by Native SAD from a dataset collected in 60 second with JUNGFRAU detector

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
AHIS297
AHIS301
AGLU320
A7MF1005

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 1002
ChainResidue
AHOH1636
ASER332
AASP333
AGLY335
AHOH1594
AHOH1612

site_idAC3
Number of Residues3
Detailsbinding site for residue DMS A 1003
ChainResidue
ATHR393
ALEU394
AASN507

site_idAC4
Number of Residues2
Detailsbinding site for residue DMS A 1004
ChainResidue
AGLU535
AHOH1211

site_idAC5
Number of Residues13
Detailsbinding site for residue 7MF A 1005
ChainResidue
AGLU121
AMET260
AALA262
AGLU264
AARG293
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
ATYR376
ATYR381
AZN1001

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW
ChainResidueDetails
AVAL294-TRP303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865
ChainResidueDetails
AGLU298

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU121
AGLY261
AHIS297
AHIS301
AGLU320

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305
ChainResidueDetails
ATYR381

227111

PDB entries from 2024-11-06

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