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2GU6

E. coli methionine aminopeptidase in complex with NleP, 1: 2, di-metalated

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008198molecular_functionferrous iron binding
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004239molecular_functioninitiator methionyl aminopeptidase activity
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008198molecular_functionferrous iron binding
B0008235molecular_functionmetalloexopeptidase activity
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 265
ChainResidue
AASP108
AHIS171
AGLU204
AGLU235
AMN266
ANLP3808

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 266
ChainResidue
AMN265
ANLP3808
AASP97
AASP108
AGLU235

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 265
ChainResidue
BASP108
BHIS171
BGLU204
BGLU235
BMN266
BNLP3808

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 266
ChainResidue
BASP97
BASP108
BGLU235
BMN265
BNLP3808

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 300
ChainResidue
AASN74
AVAL76
ASER231
AHOH3863

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 300
ChainResidue
BASN74
BVAL76
BSER231
BHOH3855

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NLP A 3808
ChainResidue
ATYR65
AHIS79
AASP97
ATHR99
AASP108
AHIS171
APHE177
AHIS178
AGLU204
AGLU235
AMN265
AMN266
AHOH3847
AHOH3901

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NLP B 3808
ChainResidue
BTYR62
BTYR65
BHIS79
BASP97
BTHR99
BASP108
BHIS171
BPHE177
BHIS178
BGLU204
BGLU235
BMN265
BMN266
BHOH3888

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGrgfHeepqVl.HY
ChainResidueDetails
ATYR168-TYR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
AHIS79
AHIS178
BHIS79
BHIS178

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729
ChainResidueDetails
AASP97
BGLU235
AASP108
AHIS171
AGLU204
AGLU235
BASP97
BASP108
BHIS171
BGLU204

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
ATHR99
BTHR99

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204
AGLN182

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU204
BGLN182

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU204

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PDB entries from 2024-07-10

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