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3MX6

Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004239molecular_functioninitiator methionyl aminopeptidase activity
B0006508biological_processproteolysis
B0008235molecular_functionmetalloexopeptidase activity
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MET A 262
ChainResidue
APHE63
AMN259
AMN260
AHOH463
AHOH532
AHOH623
AHIS77
AASP94
AASP105
AHIS168
AHIS175
AGLU201
ATRP219
AGLU233

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MET B 262
ChainResidue
BPHE63
BHIS77
BASP94
BASP105
BHIS168
BHIS175
BGLU201
BGLU233
BMN259
BMN260
BHOH346
BHOH496
BHOH625

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 259
ChainResidue
AASP105
AHIS168
AGLU201
AGLU233
AMN260
AMET262

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 260
ChainResidue
AASP94
AASP105
AGLU233
AMN259
AMET262
AHOH532

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 261
ChainResidue
AASN72
AVAL74
ASER229
AHOH269

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 259
ChainResidue
BASP105
BHIS168
BGLU201
BGLU233
BMN260
BMET262

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 260
ChainResidue
BASP94
BASP105
BGLU233
BMN259
BMET262
BHOH496

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 261
ChainResidue
BASN72
BVAL74
BSER229
BHOH270

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YtGHGIGrvfHdkpsIl.NY
ChainResidueDetails
ATYR165-TYR183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974
ChainResidueDetails
AHIS77
BHIS77

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3
ChainResidueDetails
BASP105
BHIS168
BGLU201
BGLU233
AASP94
AASP105
AHIS168
AGLU201
AGLU233
BASP94

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.3
ChainResidueDetails
AHIS175
BHIS175

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.3
ChainResidueDetails
ATRP219
BTRP219

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PDB entries from 2024-06-12

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