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4LWZ

Crystal structure of Myo5b globular tail domain in complex with inactive Rab11a

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
AGLY21
ASER40
AASN124
ALYS125
AASP127
ALEU128
ASER154
AALA155
ALEU156
AMG202
AHOH302
AVAL22
AHOH307
AHOH308
AHOH317
AGLY23
ALYS24
ASER25
AASN26
APHE36
AASN37
ALEU38

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER25
ATHR43
AGDP201
AHOH302
AHOH307
AHOH308

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP C 201
ChainResidue
CASP19
CGLY21
CVAL22
CGLY23
CLYS24
CSER25
CASN26
CPHE36
CASN37
CLEU38
CSER40
CASN124
CLYS125
CASP127
CLEU128
CSER154
CALA155
CLEU156
CMG202
CHOH301
CHOH315

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 202
ChainResidue
CSER25
CTHR43
CGDP201
CHOH301
CHOH302

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL
ChainResidueDetails
AVAL14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
ASER20
CSER20

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8
ChainResidueDetails
AGLY21
AASP127
AALA155
ALEU156
CGLY21
CGLY23
CLYS24
CASN26
CASN37
CLEU38
CSER40
AGLY23
CGLY69
CLYS125
CASP127
CALA155
CLEU156
ALYS24
AASN26
AASN37
ALEU38
ASER40
AGLY69
ALYS125

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0007744|PDB:2GZH
ChainResidueDetails
AVAL22
CVAL22

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15837192, ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:1OIX, ECO:0007744|PDB:1YZK, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH, ECO:0007744|PDB:2HV8
ChainResidueDetails
ASER25
ATHR43
CSER25
CTHR43

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
ASER42
CSER42

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD
ChainResidueDetails
AASP66
CASP66

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905101, ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, ECO:0007744|PDB:2D7C, ECO:0007744|PDB:2GZD, ECO:0007744|PDB:2GZH
ChainResidueDetails
AASN124
CASN124

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000269|Ref.11
ChainResidueDetails
AGLY2
CGLY2

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32974215
ChainResidueDetails
AARG4
CARG4

237423

PDB entries from 2025-06-11

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